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Conserved domains on  [gi|1039741797|ref|XP_017170657|]
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echinoderm microtubule-associated protein-like 1 isoform X1 [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 ...
 258-329 3.62e-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: 3.62e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741797 258 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 329
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 77-133 3.50e-35

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: 127.53  E-value: 3.50e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741797  77 DDSASAASSMEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 133
Cdd:cd21947     2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
418-769 4.84e-29

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 120.40  E-value: 4.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 418 SNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTF 496
Cdd:COG2319    97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAF 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 497 SENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgp 575
Cdd:COG2319   171 SPDGKLLaSGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD----------------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 576 irtVAEGKgnviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIE 654
Cdd:COG2319   233 ---LATGK-------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHS 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 655 DPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTR 734
Cdd:COG2319   289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1039741797 735 vgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 769
Cdd:COG2319   369 ----TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 692-884 5.36e-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: 5.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 692 HTDGneqLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVgkcsGHSSFITHLDWSVNSQFLVSNSGDYEILYWVP 771
Cdd:cd00200     8 HTGG---VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 772 SACKQVVsvettrdiewatytcTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRapsHIYS 851
Cdd:cd00200    81 ETGECVR---------------TLTGHTSYVS----------SVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLR 132

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039741797 852 GHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 884
Cdd:cd00200   133 GHTDWVNSVAFS-PDGTFVASSSQDGTIKLWDL 164
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 332-379 1.33e-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: 1.33e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039741797  332 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 379
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 258-329 3.62e-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: 3.62e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741797 258 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 329
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 77-133 3.50e-35

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: 127.53  E-value: 3.50e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741797  77 DDSASAASSMEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 133
Cdd:cd21947     2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
418-769 4.84e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 120.40  E-value: 4.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 418 SNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTF 496
Cdd:COG2319    97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAF 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 497 SENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgp 575
Cdd:COG2319   171 SPDGKLLaSGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD----------------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 576 irtVAEGKgnviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIE 654
Cdd:COG2319   233 ---LATGK-------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHS 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 655 DPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTR 734
Cdd:COG2319   289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1039741797 735 vgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 769
Cdd:COG2319   369 ----TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 335-723 2.98e-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: 2.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 335 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 409
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 410 ghLCAVddSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegnslnkkqglfekqekpk 489
Cdd:cd00200    66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 490 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKlhkaei 569
Cdd:cd00200   113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK------ 168

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 570 peqfgpirtvaegkgnviligttrnfvLQGTLSgdftpitqGHTDELWGLAIHASKPQFLTCGHDKHATLWDA------- 642
Cdd:cd00200   169 ---------------------------CVATLT--------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 643 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 720
Cdd:cd00200   214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                  ...
gi 1039741797 721 YIY 723
Cdd:cd00200   286 RIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 692-884 5.36e-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: 5.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 692 HTDGneqLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVgkcsGHSSFITHLDWSVNSQFLVSNSGDYEILYWVP 771
Cdd:cd00200     8 HTGG---VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 772 SACKQVVsvettrdiewatytcTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRapsHIYS 851
Cdd:cd00200    81 ETGECVR---------------TLTGHTSYVS----------SVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLR 132

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039741797 852 GHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 884
Cdd:cd00200   133 GHTDWVNSVAFS-PDGTFVASSSQDGTIKLWDL 164
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 332-379 1.33e-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: 1.33e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039741797  332 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 379
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
332-379 1.44e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741797 332 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 379
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 664-753 5.96e-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: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 664 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNCIYIYGVtDNGRKytrVGKCSGH 741
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDA-ENGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 1039741797 742 SSFITHLDWSVN 753
Cdd:pfam12894  80 SDLITCLGWGEN 91
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 258-329 3.62e-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: 3.62e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039741797 258 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 329
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 77-133 3.50e-35

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: 127.53  E-value: 3.50e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039741797  77 DDSASAASSMEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 133
Cdd:cd21947     2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
418-769 4.84e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 120.40  E-value: 4.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 418 SNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTF 496
Cdd:COG2319    97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAF 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 497 SENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgp 575
Cdd:COG2319   171 SPDGKLLaSGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD----------------- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 576 irtVAEGKgnviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIE 654
Cdd:COG2319   233 ---LATGK-------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHS 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 655 DPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTR 734
Cdd:COG2319   289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1039741797 735 vgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 769
Cdd:COG2319   369 ----TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 335-723 2.98e-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: 2.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 335 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 409
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 410 ghLCAVddSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegnslnkkqglfekqekpk 489
Cdd:cd00200    66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 490 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKlhkaei 569
Cdd:cd00200   113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK------ 168

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 570 peqfgpirtvaegkgnviligttrnfvLQGTLSgdftpitqGHTDELWGLAIHASKPQFLTCGHDKHATLWDA------- 642
Cdd:cd00200   169 ---------------------------CVATLT--------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 643 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 720
Cdd:cd00200   214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                  ...
gi 1039741797 721 YIY 723
Cdd:cd00200   286 RIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
323-727 2.55e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 106.53  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 323 VVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTskdgkqlpphVRIWDSVTLNTLHVIGIgfFDRAVTCIA 402
Cdd:COG2319    60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT----------VRLWDLATGLLLRTLTG--HTGAVRSVA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 403 FSKSnggGHLCAVDdSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgL 481
Cdd:COG2319   128 FSPD---GKTLASG-SADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGtVRLWDLATGKL-----L 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 482 FEKQEKPKFVLCVTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgn 560
Cdd:COG2319   198 RTLTGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTG-HSGSVRSVAFSPDGRLLASGSADGTVRLWD-- 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 561 yqklhkaeipeqfgpirtVAEGKgnviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLW 640
Cdd:COG2319   275 ------------------LATGE-------------LLRTL--------TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 641 DAVGHRPVWD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNC 719
Cdd:COG2319   316 DLATGKLLRTlTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395


                  ....*...
gi 1039741797 720 IYIYGVTD 727
Cdd:COG2319   396 VRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
414-884 3.68e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.07  E-value: 3.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 414 AVDDSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGNSLnkkqgLFEKQEKPKFVLC 493
Cdd:COG2319     9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL-----LATLLGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 494 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDG-TLVSGGGkDRRLISWNgnyqklhkaeipe 571
Cdd:COG2319    84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSA-DGTVRLWD------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 572 qfgpirtVAEGKgnviligttrnfvLQGTLSGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD- 650
Cdd:COG2319   149 -------LATGK-------------LLRTLTG--------HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 651 KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGR 730
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 731 KYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvSVETTRDIEwatytcTLGFHVFGVWpegsdgt 810
Cdd:COG2319   281 LRTL----TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW---------DLATGKLLR------TLTGHTGAVR------- 334

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039741797 811 dinAVCRAHERKLLCTGDDFGKVHLFSypcSQFRAPSHIYSGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 884
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 ...
 529-883 8.34e-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: 8.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 529 HEGGIFALCMLRDG-TLVSGGGkDRRLISWNgnyqklhkaeipeqfgpirtvaegkgnviligtTRNFVLQGTLsgdftp 607
Cdd:cd00200     8 HTGGVTCVAFSPDGkLLATGSG-DGTIKVWD---------------------------------LETGELLRTL------ 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 608 itQGHTDELWGLAIHASKPQFLTCGHDKHATLWDA---------VGHR-PVWdkiiedpaqSSGFHPSGSVVAVGTLTGR 677
Cdd:cd00200    48 --KGHTGPVRDVAASADGTYLASGSSDKTIRLWDLetgecvrtlTGHTsYVS---------SVAFSPDGRILSSSSRDKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 678 WFVFDTETKDLVTV---HTDgneqlSVM--RYSPDGNFLAIGSHDNCIYIYgvtdNGRKYTRVGKCSGHSSFITHLDWSV 752
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLW----DLRTGKCVATLTGHTGEVNSVAFSP 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 753 NSQFLVSNSGDYEILYWVPSACKQVvsvettrdiewatytCTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGK 832
Cdd:cd00200   188 DGEKLLSSSSDGTIKLWDLSTGKCL---------------GTLRGHENGVN----------SVAFSPDGYLLASGSEDGT 242

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039741797 833 VHLFSypcSQFRAPSHIYSGHSSHVTNVDFlCEDSHLISTGGKDTSIMQWR 883
Cdd:cd00200   243 IRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
539-884 3.59e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 93.82  E-value: 3.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 539 LRDGTLVSGGGKDRRLISWNGNYQKLHKAEIPEQFGPIRTVAEGKGNVILIGTTRNFVLQGTLSGDFTPITQGHTDELWG 618
Cdd:COG2319     4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 619 LAIHASKPQFLTCGHDKHATLWDAV-GHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNE 697
Cdd:COG2319    84 VAFSPDGRLLASASADGTVRLWDLAtGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 698 QLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTrvgkCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqv 777
Cdd:COG2319   164 AVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT----LTGHTGAVRSVAFSPDGKLLASGSADGTVRLW-------- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 778 vSVETTRDIewatytCTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSypcSQFRAPSHIYSGHSSHV 857
Cdd:COG2319   232 -DLATGKLL------RTLTGHSGSVR----------SVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHSGGV 291

                         330       340
                  ....*....|....*....|....*..
gi 1039741797 858 TNVDFLcEDSHLISTGGKDTSIMQWRV 884
Cdd:COG2319   292 NSVAFS-PDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 326-641 7.82e-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: 90.86  E-value: 7.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 326 LYNVE-EQLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDSVTLNTLHVIGiGFFDrAVTCIAFS 404
Cdd:cd00200    35 VWDLEtGELLRTLKGHTGPVRDVAASADGTYLASG-----SSDKT-----IRLWDLETGECVRTLT-GHTS-YVSSVAFS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 405 KSnggGHLcAVDDSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPTDTnIIVTCGKSH-LYFWTLEGNSLNKkqgLFE 483
Cdd:cd00200   103 PD---GRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT-FVASSSQDGtIKLWDLRTGKCVA---TLT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 484 KQEKPkfVLCVTFSENGDT-ITGDSSGNILVWGKGTnRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyq 562
Cdd:cd00200   175 GHTGE--VNSVAFSPDGEKlLSSSSDGTIKLWDLST-GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD---- 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039741797 563 klhkaeipeqfgpirtvaegkgnviligtTRNFVLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWD 641
Cdd:cd00200   248 -----------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 86-133 2.37e-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: 2.37e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741797  86 MEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 133
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 77-128 1.10e-17

trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm microtubule-associated protein-like 4 (EMAP-4), also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to the N-terminal trimerization domain of EMAP-4.


Pssm-ID: 409271  Cd Length: 59  Bit Score: 77.72  E-value: 1.10e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039741797  77 DDSASAASSMEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQA 128
Cdd:cd21950     4 DDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVA 55
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 86-129 6.22e-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: 6.22e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1039741797  86 MEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAV 129
Cdd:cd21931     1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 82-126 1.08e-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: 57.34  E-value: 1.08e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1039741797  82 AASSMEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQ 126
Cdd:cd21949     1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 692-884 5.36e-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: 5.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 692 HTDGneqLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVgkcsGHSSFITHLDWSVNSQFLVSNSGDYEILYWVP 771
Cdd:cd00200     8 HTGG---VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK----GHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 772 SACKQVVsvettrdiewatytcTLGFHVFGVWpegsdgtdinAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRapsHIYS 851
Cdd:cd00200    81 ETGECVR---------------TLTGHTSYVS----------SVAFSPDGRILSSSSRDKTIKVWDVETGKCL---TTLR 132

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039741797 852 GHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 884
Cdd:cd00200   133 GHTDWVNSVAFS-PDGTFVASSSQDGTIKLWDL 164
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 740-885 1.93e-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: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 740 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVCRAH 819
Cdd:cd00200     7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039741797 820 ERKLLCTGDDfGKVHLFSYpcsQFRAPSHIYSGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 885
Cdd:cd00200    63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 332-379 1.33e-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: 1.33e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039741797  332 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 379
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
332-379 1.44e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039741797 332 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 379
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 664-753 5.96e-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: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039741797 664 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNCIYIYGVtDNGRKytrVGKCSGH 741
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDA-ENGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 1039741797 742 SSFITHLDWSVN 753
Cdd:pfam12894  80 SDLITCLGWGEN 91
 
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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