NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|556503435|ref|NP_001273276|]
View 

echinoderm microtubule-associated protein-like 1 isoform 4 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 173-244 3.04e-40

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: 141.92  E-value: 3.04e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556503435  173 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 244
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
262-684 4.72e-30

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.48  E-value: 4.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 262 LAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGffDRAVTCIAFSksNGGGHLcaVDDSNDHVLSVW 341
Cdd:COG2319   32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFS--PDGRLL--ASASADGTVRLW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 342 DWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTFSENGDTI-T 419
Cdd:COG2319  106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAFSPDGKLLaS 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 420 GDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgpirtVAEGKg 499
Cdd:COG2319  180 GSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD--------------------LATGK- 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 500 nviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIEDPAQSSGFH 578
Cdd:COG2319  238 ------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFS 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 579 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRvgkcSGHSS 658
Cdd:COG2319  298 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL----TGHTG 373

                        410       420
                 ....*....|....*....|....*.
gi 556503435 659 FITHLDWSVNSQFLVSNSGDYEILYW 684
Cdd:COG2319  374 AVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP-like super family cl41737
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 1-48 1.14e-28

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.


The actual alignment was detected with superfamily member cd21947:

Pssm-ID: 425368  Cd Length: 58  Bit Score: 108.65  E-value: 1.14e-28
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 556503435   1 MEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 48
Cdd:cd21947   11 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 607-799 4.22e-10

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: 61.58  E-value: 4.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 607 HTDGneqLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVgkcsGHSSFITHLDWSVNSQFLVSNSGDYEILYWVP 686
Cdd:cd00200    8 HTGG---VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 687 SACKQVVsvettrdiewatytcTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRapsHIYS 766
Cdd:cd00200   81 ETGECVR---------------TLTGHTSYVS----------SVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLR 132

                        170       180       190
                 ....*....|....*....|....*....|...
gi 556503435 767 GHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 799
Cdd:cd00200  133 GHTDWVNSVAFS-PDGTFVASSSQDGTIKLWDL 164
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 173-244 3.04e-40

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: 141.92  E-value: 3.04e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556503435  173 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 244
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
262-684 4.72e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.48  E-value: 4.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 262 LAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGffDRAVTCIAFSksNGGGHLcaVDDSNDHVLSVW 341
Cdd:COG2319   32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFS--PDGRLL--ASASADGTVRLW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 342 DWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTFSENGDTI-T 419
Cdd:COG2319  106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAFSPDGKLLaS 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 420 GDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgpirtVAEGKg 499
Cdd:COG2319  180 GSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD--------------------LATGK- 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 500 nviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIEDPAQSSGFH 578
Cdd:COG2319  238 ------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFS 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 579 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRvgkcSGHSS 658
Cdd:COG2319  298 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL----TGHTG 373

                        410       420
                 ....*....|....*....|....*.
gi 556503435 659 FITHLDWSVNSQFLVSNSGDYEILYW 684
Cdd:COG2319  374 AVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 1-48 1.14e-28

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: 108.65  E-value: 1.14e-28
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 556503435   1 MEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 48
Cdd:cd21947   11 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 250-638 2.28e-26

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 109.73  E-value: 2.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 250 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 324
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 325 ghLCAVddSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegnslnkkqglfekqekpk 404
Cdd:cd00200   66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 405 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKlhkaei 484
Cdd:cd00200  113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK------ 168

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 485 peqfgpirtvaegkgnviligttrnfvLQGTLSgdftpitqGHTDELWGLAIHASKPQFLTCGHDKHATLWDA------- 557
Cdd:cd00200  169 ---------------------------CVATLT--------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 558 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 635
Cdd:cd00200  214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                 ...
gi 556503435 636 YIY 638
Cdd:cd00200  286 RIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 607-799 4.22e-10

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: 61.58  E-value: 4.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 607 HTDGneqLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVgkcsGHSSFITHLDWSVNSQFLVSNSGDYEILYWVP 686
Cdd:cd00200    8 HTGG---VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 687 SACKQVVsvettrdiewatytcTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRapsHIYS 766
Cdd:cd00200   81 ETGECVR---------------TLTGHTSYVS----------SVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLR 132

                        170       180       190
                 ....*....|....*....|....*....|...
gi 556503435 767 GHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 799
Cdd:cd00200  133 GHTDWVNSVAFS-PDGTFVASSSQDGTIKLWDL 164
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 247-294 1.20e-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: 37.29  E-value: 1.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 556503435   247 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 294
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
247-294 1.27e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 556503435  247 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 294
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 173-244 3.04e-40

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: 141.92  E-value: 3.04e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556503435  173 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 244
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
262-684 4.72e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.48  E-value: 4.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 262 LAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGffDRAVTCIAFSksNGGGHLcaVDDSNDHVLSVW 341
Cdd:COG2319   32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFS--PDGRLL--ASASADGTVRLW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 342 DWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTFSENGDTI-T 419
Cdd:COG2319  106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAFSPDGKLLaS 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 420 GDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgpirtVAEGKg 499
Cdd:COG2319  180 GSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD--------------------LATGK- 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 500 nviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIEDPAQSSGFH 578
Cdd:COG2319  238 ------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFS 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 579 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRvgkcSGHSS 658
Cdd:COG2319  298 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL----TGHTG 373

                        410       420
                 ....*....|....*....|....*.
gi 556503435 659 FITHLDWSVNSQFLVSNSGDYEILYW 684
Cdd:COG2319  374 AVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 1-48 1.14e-28

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: 108.65  E-value: 1.14e-28
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 556503435   1 MEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 48
Cdd:cd21947   11 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 250-638 2.28e-26

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 109.73  E-value: 2.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 250 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 324
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 325 ghLCAVddSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegnslnkkqglfekqekpk 404
Cdd:cd00200   66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 405 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKlhkaei 484
Cdd:cd00200  113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK------ 168

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 485 peqfgpirtvaegkgnviligttrnfvLQGTLSgdftpitqGHTDELWGLAIHASKPQFLTCGHDKHATLWDA------- 557
Cdd:cd00200  169 ---------------------------CVATLT--------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 558 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 635
Cdd:cd00200  214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                 ...
gi 556503435 636 YIY 638
Cdd:cd00200  286 RIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
238-642 3.23e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 3.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 238 VVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTskdgkqlpphVRIWDSVTLNTLHVIGIgfFDRAVTCIA 317
Cdd:COG2319   60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT----------VRLWDLATGLLLRTLTG--HTGAVRSVA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 318 FSKSnggGHLCAVDdSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgL 396
Cdd:COG2319  128 FSPD---GKTLASG-SADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGtVRLWDLATGKL-----L 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 397 FEKQEKPKFVLCVTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgn 475
Cdd:COG2319  198 RTLTGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTG-HSGSVRSVAFSPDGRLLASGSADGTVRLWD-- 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 476 yqklhkaeipeqfgpirtVAEGKgnviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLW 555
Cdd:COG2319  275 ------------------LATGE-------------LLRTL--------TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 556 DAVGHRPVWD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNC 634
Cdd:COG2319  316 DLATGKLLRTlTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395


                 ....*...
gi 556503435 635 IYIYGVTD 642
Cdd:COG2319  396 VRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
329-799 3.94e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 105.76  E-value: 3.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 329 AVDDSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGNSLnkkqgLFEKQEKPKFVLC 408
Cdd:COG2319    9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL-----LATLLGHTAAVLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 409 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDG-TLVSGGGkDRRLISWNgnyqklhkaeipe 486
Cdd:COG2319   84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSA-DGTVRLWD------------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 487 qfgpirtVAEGKgnviligttrnfvLQGTLSGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD- 565
Cdd:COG2319  149 -------LATGK-------------LLRTLTG--------HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 566 KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGR 645
Cdd:COG2319  201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 646 KYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvSVETTRDIEwatytcTLGFHVFGVWpegsdgt 725
Cdd:COG2319  281 LRTL----TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW---------DLATGKLLR------TLTGHTGAVR------- 334

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556503435 726 dinAVCRAHERKLLCTGDDFGKVHLFSypcSQFRAPSHIYSGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 799
Cdd:COG2319  335 ---SVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFS-PDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 444-798 6.16e-21

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: 93.94  E-value: 6.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 444 HEGGIFALCMLRDG-TLVSGGGkDRRLISWNgnyqklhkaeipeqfgpirtvaegkgnviligtTRNFVLQGTLsgdftp 522
Cdd:cd00200    8 HTGGVTCVAFSPDGkLLATGSG-DGTIKVWD---------------------------------LETGELLRTL------ 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 523 itQGHTDELWGLAIHASKPQFLTCGHDKHATLWDA---------VGHR-PVWdkiiedpaqSSGFHPSGSVVAVGTLTGR 592
Cdd:cd00200   48 --KGHTGPVRDVAASADGTYLASGSSDKTIRLWDLetgecvrtlTGHTsYVS---------SVAFSPDGRILSSSSRDKT 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 593 WFVFDTETKDLVTV---HTDgneqlSVM--RYSPDGNFLAIGSHDNCIYIYgvtdNGRKYTRVGKCSGHSSFITHLDWSV 667
Cdd:cd00200  117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLW----DLRTGKCVATLTGHTGEVNSVAFSP 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 668 NSQFLVSNSGDYEILYWVPSACKQVvsvettrdiewatytCTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGK 747
Cdd:cd00200  188 DGEKLLSSSSDGTIKLWDLSTGKCL---------------GTLRGHENGVN----------SVAFSPDGYLLASGSEDGT 242

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 556503435 748 VHLFSypcSQFRAPSHIYSGHSSHVTNVDFlCEDSHLISTGGKDTSIMQWR 798
Cdd:cd00200  243 IRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
454-799 7.84e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 95.75  E-value: 7.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 454 LRDGTLVSGGGKDRRLISWNGNYQKLHKAEIPEQFGPIRTVAEGKGNVILIGTTRNFVLQGTLSGDFTPITQGHTDELWG 533
Cdd:COG2319    4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 534 LAIHASKPQFLTCGHDKHATLWDAV-GHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNE 612
Cdd:COG2319   84 VAFSPDGRLLASASADGTVRLWDLAtGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 613 QLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTrvgkCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqv 692
Cdd:COG2319  164 AVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLW-------- 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 693 vSVETTRDIewatytCTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSypcSQFRAPSHIYSGHSSHV 772
Cdd:COG2319  232 -DLATGKLL------RTLTGHSGSVR----------SVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHSGGV 291

                        330       340
                 ....*....|....*....|....*..
gi 556503435 773 TNVDFLcEDSHLISTGGKDTSIMQWRV 799
Cdd:COG2319  292 NSVAFS-PDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 241-556 5.57e-20

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 91.24  E-value: 5.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 241 LYNVE-EQLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDSVTLNTLHVIGiGFFDrAVTCIAFS 319
Cdd:cd00200   35 VWDLEtGELLRTLKGHTGPVRDVAASADGTYLASG-----SSDKT-----IRLWDLETGECVRTLT-GHTS-YVSSVAFS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 320 KSnggGHLcAVDDSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPTDTnIIVTCGKSH-LYFWTLEGNSLNKkqgLFE 398
Cdd:cd00200  103 PD---GRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT-FVASSSQDGtIKLWDLRTGKCVA---TLT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 399 KQEKPkfVLCVTFSENGDT-ITGDSSGNILVWGKGTnRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyq 477
Cdd:cd00200  175 GHTGE--VNSVAFSPDGEKlLSSSSDGTIKLWDLST-GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD---- 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556503435 478 klhkaeipeqfgpirtvaegkgnviligtTRNFVLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWD 556
Cdd:cd00200  248 -----------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 1-48 2.14e-18

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: 79.10  E-value: 2.14e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 556503435   1 MEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 48
Cdd:cd21948    1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 1-44 5.63e-17

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: 74.88  E-value: 5.63e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 556503435   1 MEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAV 44
Cdd:cd21931    1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 2-43 1.96e-13

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: 65.39  E-value: 1.96e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 556503435   2 EVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQA 43
Cdd:cd21950   14 DVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVA 55
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 5-41 2.63e-10

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: 56.18  E-value: 2.63e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556503435   5 DRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQ 41
Cdd:cd21949    9 DPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 607-799 4.22e-10

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: 61.58  E-value: 4.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 607 HTDGneqLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVgkcsGHSSFITHLDWSVNSQFLVSNSGDYEILYWVP 686
Cdd:cd00200    8 HTGG---VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 687 SACKQVVsvettrdiewatytcTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRapsHIYS 766
Cdd:cd00200   81 ETGECVR---------------TLTGHTSYVS----------SVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLR 132

                        170       180       190
                 ....*....|....*....|....*....|...
gi 556503435 767 GHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 799
Cdd:cd00200  133 GHTDWVNSVAFS-PDGTFVASSSQDGTIKLWDL 164
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 655-800 1.62e-08

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: 56.57  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435 655 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVCRAH 734
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556503435 735 ERKLLCTGDDfGKVHLFSYpcsQFRAPSHIYSGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 800
Cdd:cd00200   63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 247-294 1.20e-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: 37.29  E-value: 1.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 556503435   247 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 294
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
247-294 1.27e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 556503435  247 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 294
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 579-668 4.54e-03

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 36.87  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503435  579 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNCIYIYGVtDNGRKytrVGKCSGH 656
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDA-ENGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 556503435  657 SSFITHLDWSVN 668
Cdd:pfam12894  80 SDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 525-556 9.14e-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: 34.60  E-value: 9.14e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 556503435   525 QGHTDELWGLAIHASKPQFLTCGHDKHATLWD 556
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH