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Conserved domains on  [gi|1399236783|ref|NP_001351126|]
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echinoderm microtubule-associated protein-like 1 isoform 2 [Mus musculus]

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 ...
 156-227 2.90e-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: 2.90e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1399236783 156 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 227
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
245-667 7.18e-30

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.71  E-value: 7.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 245 LAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGffDRAVTCIAFSksNGGGHLcaVDDSNDHVLSVW 324
Cdd:COG2319    32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFS--PDGRLL--ASASADGTVRLW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 325 DWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTFSENGDTI-T 402
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAFSPDGKLLaS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 403 GDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgpirtVAEGKg 482
Cdd:COG2319   180 GSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD--------------------LATGK- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 483 nviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIEDPAQSSGFH 561
Cdd:COG2319   238 ------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 562 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRvgkcSGHSS 641
Cdd:COG2319   298 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL----TGHTG 373

                         410       420
                  ....*....|....*....|....*.
gi 1399236783 642 FITHLDWSVNSQFLVSNSGDYEILYW 667
Cdd:COG2319   374 AVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP-like super family cl41737
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 1-48 1.11e-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: 1.11e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1399236783   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 ...
 590-782 4.63e-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: 4.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 590 HTDGneqLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVgkcsGHSSFITHLDWSVNSQFLVSNSGDYEILYWVP 669
Cdd:cd00200     8 HTGG---VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 670 SACKQVVsvettrdiewatytcTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRapsHIYS 749
Cdd:cd00200    81 ETGECVR---------------TLTGHTSYVS----------SVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLR 132

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1399236783 750 GHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 782
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 ...
 156-227 2.90e-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: 2.90e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1399236783 156 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 227
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
245-667 7.18e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.71  E-value: 7.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 245 LAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGffDRAVTCIAFSksNGGGHLcaVDDSNDHVLSVW 324
Cdd:COG2319    32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFS--PDGRLL--ASASADGTVRLW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 325 DWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTFSENGDTI-T 402
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAFSPDGKLLaS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 403 GDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgpirtVAEGKg 482
Cdd:COG2319   180 GSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD--------------------LATGK- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 483 nviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIEDPAQSSGFH 561
Cdd:COG2319   238 ------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 562 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRvgkcSGHSS 641
Cdd:COG2319   298 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL----TGHTG 373

                         410       420
                  ....*....|....*....|....*.
gi 1399236783 642 FITHLDWSVNSQFLVSNSGDYEILYW 667
Cdd:COG2319   374 AVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 1-48 1.11e-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: 1.11e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1399236783   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 ...
 233-621 3.06e-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: 109.35  E-value: 3.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 233 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 307
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 308 ghLCAVddSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegnslnkkqglfekqekpk 387
Cdd:cd00200    66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 388 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKlhkaei 467
Cdd:cd00200   113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK------ 168

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 468 peqfgpirtvaegkgnviligttrnfvLQGTLSgdftpitqGHTDELWGLAIHASKPQFLTCGHDKHATLWDA------- 540
Cdd:cd00200   169 ---------------------------CVATLT--------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 541 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 618
Cdd:cd00200   214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                  ...
gi 1399236783 619 YIY 621
Cdd:cd00200   286 RIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 590-782 4.63e-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: 4.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 590 HTDGneqLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVgkcsGHSSFITHLDWSVNSQFLVSNSGDYEILYWVP 669
Cdd:cd00200     8 HTGG---VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 670 SACKQVVsvettrdiewatytcTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRapsHIYS 749
Cdd:cd00200    81 ETGECVR---------------TLTGHTSYVS----------SVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLR 132

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1399236783 750 GHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 782
Cdd:cd00200   133 GHTDWVNSVAFS-PDGTFVASSSQDGTIKLWDL 164
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 230-277 1.25e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 36.91  E-value: 1.25e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1399236783  230 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 277
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
230-277 1.33e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1399236783 230 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 277
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 ...
 156-227 2.90e-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: 2.90e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1399236783 156 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 227
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
245-667 7.18e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.71  E-value: 7.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 245 LAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGffDRAVTCIAFSksNGGGHLcaVDDSNDHVLSVW 324
Cdd:COG2319    32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFS--PDGRLL--ASASADGTVRLW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 325 DWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTFSENGDTI-T 402
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAFSPDGKLLaS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 403 GDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgpirtVAEGKg 482
Cdd:COG2319   180 GSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD--------------------LATGK- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 483 nviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIEDPAQSSGFH 561
Cdd:COG2319   238 ------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 562 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRvgkcSGHSS 641
Cdd:COG2319   298 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL----TGHTG 373

                         410       420
                  ....*....|....*....|....*.
gi 1399236783 642 FITHLDWSVNSQFLVSNSGDYEILYW 667
Cdd:COG2319   374 AVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 1-48 1.11e-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: 1.11e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1399236783   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 ...
 233-621 3.06e-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: 109.35  E-value: 3.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 233 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 307
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 308 ghLCAVddSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegnslnkkqglfekqekpk 387
Cdd:cd00200    66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 388 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKlhkaei 467
Cdd:cd00200   113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK------ 168

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 468 peqfgpirtvaegkgnviligttrnfvLQGTLSgdftpitqGHTDELWGLAIHASKPQFLTCGHDKHATLWDA------- 540
Cdd:cd00200   169 ---------------------------CVATLT--------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 541 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 618
Cdd:cd00200   214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                  ...
gi 1399236783 619 YIY 621
Cdd:cd00200   286 RIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
221-625 4.73e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.46  E-value: 4.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 221 VVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTskdgkqlpphVRIWDSVTLNTLHVIGIgfFDRAVTCIA 300
Cdd:COG2319    60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT----------VRLWDLATGLLLRTLTG--HTGAVRSVA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 301 FSKSnggGHLCAVDdSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgL 379
Cdd:COG2319   128 FSPD---GKTLASG-SADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGtVRLWDLATGKL-----L 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 380 FEKQEKPKFVLCVTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgn 458
Cdd:COG2319   198 RTLTGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTG-HSGSVRSVAFSPDGRLLASGSADGTVRLWD-- 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 459 yqklhkaeipeqfgpirtVAEGKgnviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLW 538
Cdd:COG2319   275 ------------------LATGE-------------LLRTL--------TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 539 DAVGHRPVWD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNC 617
Cdd:COG2319   316 DLATGKLLRTlTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395


                  ....*...
gi 1399236783 618 IYIYGVTD 625
Cdd:COG2319   396 VRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
312-782 5.65e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.99  E-value: 5.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 312 AVDDSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGNSLnkkqgLFEKQEKPKFVLC 391
Cdd:COG2319     9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL-----LATLLGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 392 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDG-TLVSGGGkDRRLISWNgnyqklhkaeipe 469
Cdd:COG2319    84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSA-DGTVRLWD------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 470 qfgpirtVAEGKgnviligttrnfvLQGTLSGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD- 548
Cdd:COG2319   149 -------LATGK-------------LLRTLTG--------HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 549 KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGR 628
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 629 KYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvSVETTRDIEwatytcTLGFHVFGVWpegsdgt 708
Cdd:COG2319   281 LRTL----TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW---------DLATGKLLR------TLTGHTGAVR------- 334

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1399236783 709 dinAVCRAHERKLLCTGDDFGKVHLFSypcSQFRAPSHIYSGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 782
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 ...
 427-781 7.94e-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: 93.55  E-value: 7.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 427 HEGGIFALCMLRDG-TLVSGGGkDRRLISWNgnyqklhkaeipeqfgpirtvaegkgnviligtTRNFVLQGTLsgdftp 505
Cdd:cd00200     8 HTGGVTCVAFSPDGkLLATGSG-DGTIKVWD---------------------------------LETGELLRTL------ 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 506 itQGHTDELWGLAIHASKPQFLTCGHDKHATLWDA---------VGHR-PVWdkiiedpaqSSGFHPSGSVVAVGTLTGR 575
Cdd:cd00200    48 --KGHTGPVRDVAASADGTYLASGSSDKTIRLWDLetgecvrtlTGHTsYVS---------SVAFSPDGRILSSSSRDKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 576 WFVFDTETKDLVTV---HTDgneqlSVM--RYSPDGNFLAIGSHDNCIYIYgvtdNGRKYTRVGKCSGHSSFITHLDWSV 650
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLW----DLRTGKCVATLTGHTGEVNSVAFSP 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 651 NSQFLVSNSGDYEILYWVPSACKQVvsvettrdiewatytCTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGK 730
Cdd:cd00200   188 DGEKLLSSSSDGTIKLWDLSTGKCL---------------GTLRGHENGVN----------SVAFSPDGYLLASGSEDGT 242

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1399236783 731 VHLFSypcSQFRAPSHIYSGHSSHVTNVDFlCEDSHLISTGGKDTSIMQWR 781
Cdd:cd00200   243 IRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
437-782 1.05e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 95.36  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 437 LRDGTLVSGGGKDRRLISWNGNYQKLHKAEIPEQFGPIRTVAEGKGNVILIGTTRNFVLQGTLSGDFTPITQGHTDELWG 516
Cdd:COG2319     4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 517 LAIHASKPQFLTCGHDKHATLWDAV-GHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNE 595
Cdd:COG2319    84 VAFSPDGRLLASASADGTVRLWDLAtGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 596 QLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTrvgkCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqv 675
Cdd:COG2319   164 AVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLW-------- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 676 vSVETTRDIewatytCTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSypcSQFRAPSHIYSGHSSHV 755
Cdd:COG2319   232 -DLATGKLL------RTLTGHSGSVR----------SVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHSGGV 291

                         330       340
                  ....*....|....*....|....*..
gi 1399236783 756 TNVDFLcEDSHLISTGGKDTSIMQWRV 782
Cdd:COG2319   292 NSVAFS-PDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 224-539 7.65e-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: 90.47  E-value: 7.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 224 LYNVE-EQLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDSVTLNTLHVIGiGFFDrAVTCIAFS 302
Cdd:cd00200    35 VWDLEtGELLRTLKGHTGPVRDVAASADGTYLASG-----SSDKT-----IRLWDLETGECVRTLT-GHTS-YVSSVAFS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 303 KSnggGHLcAVDDSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPTDTnIIVTCGKSH-LYFWTLEGNSLNKkqgLFE 381
Cdd:cd00200   103 PD---GRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT-FVASSSQDGtIKLWDLRTGKCVA---TLT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 382 KQEKPkfVLCVTFSENGDT-ITGDSSGNILVWGKGTnRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyq 460
Cdd:cd00200   175 GHTGE--VNSVAFSPDGEKlLSSSSDGTIKLWDLST-GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD---- 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1399236783 461 klhkaeipeqfgpirtvaegkgnviligtTRNFVLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWD 539
Cdd:cd00200   248 -----------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 1-48 2.10e-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: 2.10e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1399236783   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 5.51e-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: 5.51e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1399236783   1 MEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAV 44
Cdd:cd21931     1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 2-43 1.92e-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: 1.92e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1399236783   2 EVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQA 43
Cdd:cd21950    14 DVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVA 55
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 5-41 2.57e-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: 2.57e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1399236783   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 ...
 590-782 4.63e-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: 4.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 590 HTDGneqLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVgkcsGHSSFITHLDWSVNSQFLVSNSGDYEILYWVP 669
Cdd:cd00200     8 HTGG---VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 670 SACKQVVsvettrdiewatytcTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRapsHIYS 749
Cdd:cd00200    81 ETGECVR---------------TLTGHTSYVS----------SVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLR 132

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1399236783 750 GHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 782
Cdd:cd00200   133 GHTDWVNSVAFS-PDGTFVASSSQDGTIKLWDL 164
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 638-783 1.79e-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: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 638 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVCRAH 717
Cdd:cd00200     7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1399236783 718 ERKLLCTGDDfGKVHLFSYpcsQFRAPSHIYSGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 783
Cdd:cd00200    63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 230-277 1.25e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 36.91  E-value: 1.25e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1399236783  230 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 277
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
230-277 1.33e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1399236783 230 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 277
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 562-651 4.94e-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: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399236783 562 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNCIYIYGVtDNGRKytrVGKCSGH 639
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDA-ENGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 1399236783 640 SSFITHLDWSVN 651
Cdd:pfam12894  80 SDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 508-539 9.12e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.60  E-value: 9.12e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1399236783  508 QGHTDELWGLAIHASKPQFLTCGHDKHATLWD 539
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.
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