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Conserved domains on  [gi|942127551|ref|XP_014340680|]
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echinoderm microtubule-associated protein-like 1 isoform X4 [Latimeria chalumnae]

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 ...
 197-268 4.59e-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: 141.54  E-value: 4.59e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942127551  197 KMFLRGRPVTMYMPRNQVESYSLEAKSELPAKKLKLEWVYGYRGRDCRSNLYLLPTGETVYFIASVVVLYNV 268
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 22-79 1.40e-37

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: 134.08  E-value: 1.40e-37
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 942127551  22 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 79
Cdd:cd21947    1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
357-708 1.05e-29

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.33  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 357 SNDHILSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNVIVTCGKSH-LYFWTLEGGSLnkkqgLFEKQEKPKFVLCVTF 435
Cdd:COG2319   97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAF 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 436 SENGDTI-TGDSSGNILIWGKGTNRISYAIQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWTrnyqkicetevpeqfgp 514
Cdd:COG2319  171 SPDGKLLaSGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD----------------- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 515 vrtVAEGKgevvligttrnfvLQGTLsgdfhpitQGHTDELWGLAVHPVKAAFLTCGHDKHITLWDSTTHQPIWD-KLIE 593
Cdd:COG2319  233 ---LATGK-------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHS 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 594 DPAQSAGFHPSGSVIAIGTLTGRWFVLDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNYIYIYGVSENGrkysR 673
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGE----L 364

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 942127551 674 IGKCSGHSSFITHLDWCVDSKHLISNSGDYEILYW 708
Cdd:COG2319  365 LRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 679-824 7.50e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 54.65  E-value: 7.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 679 GHSSFITHLDWCVDSKHLISNSGDYEILYWissvckqlvnvDITRGiewaTYTCTLGFHVFGVWpegsdgtdiNAVCRSQ 758
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW-----------DLETG----ELLRTLKGHTGPVR---------DVAASAD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942127551 759 GKKLLSTGDDfGKVHLFSYpcsQFRAPSHVYGGHSSHVTNVNFLyDDSHLISTGGKDMSIMQWRVI 824
Cdd:cd00200   63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 271-318 2.61e-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: 36.14  E-value: 2.61e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 942127551   271 QLQRHYTSHTDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRVWD 318
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 ...
 197-268 4.59e-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: 141.54  E-value: 4.59e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942127551  197 KMFLRGRPVTMYMPRNQVESYSLEAKSELPAKKLKLEWVYGYRGRDCRSNLYLLPTGETVYFIASVVVLYNV 268
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 22-79 1.40e-37

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: 134.08  E-value: 1.40e-37
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 942127551  22 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 79
Cdd:cd21947    1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
357-708 1.05e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.33  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 357 SNDHILSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNVIVTCGKSH-LYFWTLEGGSLnkkqgLFEKQEKPKFVLCVTF 435
Cdd:COG2319   97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAF 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 436 SENGDTI-TGDSSGNILIWGKGTNRISYAIQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWTrnyqkicetevpeqfgp 514
Cdd:COG2319  171 SPDGKLLaSGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD----------------- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 515 vrtVAEGKgevvligttrnfvLQGTLsgdfhpitQGHTDELWGLAVHPVKAAFLTCGHDKHITLWDSTTHQPIWD-KLIE 593
Cdd:COG2319  233 ---LATGK-------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHS 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 594 DPAQSAGFHPSGSVIAIGTLTGRWFVLDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNYIYIYGVSENGrkysR 673
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGE----L 364

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 942127551 674 IGKCSGHSSFITHLDWCVDSKHLISNSGDYEILYW 708
Cdd:COG2319  365 LRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 274-708 1.55e-24

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: 104.34  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 274 RHYTSHTDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRVWDSVSLNTLHVI-GMGFFDRAVTCIAFSKSnggstLC 352
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLkGHTGPVRDVAASADGTY-----LA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 353 AVddSNDHILSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNVIVTCGkshlyfwtleggslnkkqglfekqekpkfvlc 432
Cdd:cd00200   68 SG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS-------------------------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 433 vtfsengdtitgdSSGNILIWGKGTNRISYAIQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWTrnyqkicetevpeqf 512
Cdd:cd00200  113 -------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWD--------------- 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 513 gpvrtvaegkgevvligtTRNFVLQGTLSGdfhpitqgHTDELWGLAVHPVKAAFLTCGHDKHITLWDSTTHQpiwdkli 592
Cdd:cd00200  164 ------------------LRTGKCVATLTG--------HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK------- 210

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 593 edpaqsagfhpsgsviAIGTLTGrwfvldtetkdlvtvHTDGneqLSVMRYSPDGNFLAIGSHDNYIYIYgvseNGRKYS 672
Cdd:cd00200  211 ----------------CLGTLRG---------------HENG---VNSVAFSPDGYLLASGSEDGTIRVW----DLRTGE 252

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 942127551 673 RIGKCSGHSSFITHLDWCVDSKHLISNSGDYEILYW 708
Cdd:cd00200  253 CVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 679-824 7.50e-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: 54.65  E-value: 7.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 679 GHSSFITHLDWCVDSKHLISNSGDYEILYWissvckqlvnvDITRGiewaTYTCTLGFHVFGVWpegsdgtdiNAVCRSQ 758
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW-----------DLETG----ELLRTLKGHTGPVR---------DVAASAD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942127551 759 GKKLLSTGDDfGKVHLFSYpcsQFRAPSHVYGGHSSHVTNVNFLyDDSHLISTGGKDMSIMQWRVI 824
Cdd:cd00200   63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 603-692 2.73e-04

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: 40.72  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551  603 PSGSVIAIGTLTGRWFVLDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNYIYIYGVsENGRKysrIGKCSGH 680
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDA-ENGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 942127551  681 SSFITHLDWCVD 692
Cdd:pfam12894  80 SDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 271-318 2.61e-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: 36.14  E-value: 2.61e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 942127551   271 QLQRHYTSHTDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRVWD 318
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
271-318 3.01e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 3.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 942127551  271 QLQRHYTSHTDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRVWD 318
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 549-580 7.00e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.98  E-value: 7.00e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 942127551   549 QGHTDELWGLAVHPVKAAFLTCGHDKHITLWD 580
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 197-268 4.59e-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: 141.54  E-value: 4.59e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942127551  197 KMFLRGRPVTMYMPRNQVESYSLEAKSELPAKKLKLEWVYGYRGRDCRSNLYLLPTGETVYFIASVVVLYNV 268
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 22-79 1.40e-37

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: 134.08  E-value: 1.40e-37
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 942127551  22 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 79
Cdd:cd21947    1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
357-708 1.05e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.33  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 357 SNDHILSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNVIVTCGKSH-LYFWTLEGGSLnkkqgLFEKQEKPKFVLCVTF 435
Cdd:COG2319   97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAF 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 436 SENGDTI-TGDSSGNILIWGKGTNRISYAIQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWTrnyqkicetevpeqfgp 514
Cdd:COG2319  171 SPDGKLLaSGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD----------------- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 515 vrtVAEGKgevvligttrnfvLQGTLsgdfhpitQGHTDELWGLAVHPVKAAFLTCGHDKHITLWDSTTHQPIWD-KLIE 593
Cdd:COG2319  233 ---LATGK-------------LLRTL--------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHS 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 594 DPAQSAGFHPSGSVIAIGTLTGRWFVLDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNYIYIYGVSENGrkysR 673
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGE----L 364

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 942127551 674 IGKCSGHSSFITHLDWCVDSKHLISNSGDYEILYW 708
Cdd:COG2319  365 LRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 COG2319
WD40 repeat [General function prediction only];
262-665 6.89e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 113.85  E-value: 6.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 262 VVVLYNVEEQLQRHYTSHTDDVKCLAVHPDRITIATGQVAGTskdgkqlpphVRVWDSVSLNTLHVIGmgFFDRAVTCIA 341
Cdd:COG2319   60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT----------VRLWDLATGLLLRTLT--GHTGAVRSVA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 342 FSkSNGGSTLCAvddSNDHILSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNVIVTCGKSH-LYFWTLEGGSLnkkqgL 420
Cdd:COG2319  128 FS-PDGKTLASG---SADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGtVRLWDLATGKL-----L 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 421 FEKQEKPKFVLCVTFSENGDTI-TGDSSGNILIWGKGTNRISYAIQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWTrn 499
Cdd:COG2319  198 RTLTGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTG-HSGSVRSVAFSPDGRLLASGSADGTVRLWD-- 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 500 yqkicetevpeqfgpvrtVAEGKgevvligttrnfvLQGTLsgdfhpitQGHTDELWGLAVHPVKAAFLTCGHDKHITLW 579
Cdd:COG2319  275 ------------------LATGE-------------LLRTL--------TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 580 DSTTHQPIWD-KLIEDPAQSAGFHPSGSVIAIGTLTGRWFVLDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNY 658
Cdd:COG2319  316 DLATGKLLRTlTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395


                 ....*..
gi 942127551 659 IYIYGVS 665
Cdd:COG2319  396 VRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
353-823 7.44e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.77  E-value: 7.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 353 AVDDSNDHILSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNVIVTCGKSHLYFWTLEGGSLnkkqgLFEKQEKPKFVLC 432
Cdd:COG2319    9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL-----LATLLGHTAAVLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 433 VTFSENGDTI-TGDSSGNILIWGKGTNRISYAIQGaHEGGIFALCMLRDG-TLVSGGGkDRKLISWTrnyqkicetevpe 510
Cdd:COG2319   84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSA-DGTVRLWD------------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 511 qfgpvrtVAEGKgevvligttrnfvLQGTLSGdfhpitqgHTDELWGLAVHPVKAAFLTCGHDKHITLWDSTTHQPIWD- 589
Cdd:COG2319  149 -------LATGK-------------LLRTLTG--------HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 590 KLIEDPAQSAGFHPSGSVIAIGTLTGRWFVLDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNYIYIYGVSENgr 669
Cdd:COG2319  201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-- 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 670 kySRIGKCSGHSSFITHLDWCVDSKHLISNSGDYEILYWissvckqlvnvditrgiEWATYTC--TLGFHVFGVWpegsd 747
Cdd:COG2319  279 --ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW-----------------DLATGKLlrTLTGHTGAVR----- 334

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942127551 748 gtdinAVCRS-QGKKLLSTGDDfGKVHLFSypcSQFRAPSHVYGGHSSHVTNVNFLYDDSHLIStGGKDMSIMQWRV 823
Cdd:COG2319  335 -----SVAFSpDGKTLASGSDD-GTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
263-583 3.55e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 3.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 263 VVLYNVE-EQLQRHYTSHTDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRVWDSVSLNTLHVIGMGffDRAVTCIA 341
Cdd:COG2319  102 VRLWDLAtGLLLRTLTGHTGAVRSVAFSPDGKTLASG-----SADGT-----VRLWDLATGKLLRTLTGH--SGAVTSVA 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 342 FSKSngGSTLcaVDDSNDHILSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNVIVTCGKSH-LYFWTLEGGSLnkkqgL 420
Cdd:COG2319  170 FSPD--GKLL--ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATGKL-----L 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 421 FEKQEKPKFVLCVTFSENGDTI-TGDSSGNILIWGKGTNRISYAIQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWTRN 499
Cdd:COG2319  240 RTLTGHSGSVRSVAFSPDGRLLaSGSADGTVRLWDLATGELLRTLTG-HSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 500 YQKiCETEVPEQFGPVRTVA-EGKGEVVLIGTTRNFV-LQGTLSGDFHPITQGHTDELWGLAVHPVKAAFLTCGHDKHIT 577
Cdd:COG2319  319 TGK-LLRTLTGHTGAVRSVAfSPDGKTLASGSDDGTVrLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVR 397


                 ....*.
gi 942127551 578 LWDSTT 583
Cdd:COG2319  398 LWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 274-708 1.55e-24

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: 104.34  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 274 RHYTSHTDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRVWDSVSLNTLHVI-GMGFFDRAVTCIAFSKSnggstLC 352
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLkGHTGPVRDVAASADGTY-----LA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 353 AVddSNDHILSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNVIVTCGkshlyfwtleggslnkkqglfekqekpkfvlc 432
Cdd:cd00200   68 SG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS-------------------------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 433 vtfsengdtitgdSSGNILIWGKGTNRISYAIQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWTrnyqkicetevpeqf 512
Cdd:cd00200  113 -------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWD--------------- 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 513 gpvrtvaegkgevvligtTRNFVLQGTLSGdfhpitqgHTDELWGLAVHPVKAAFLTCGHDKHITLWDSTTHQpiwdkli 592
Cdd:cd00200  164 ------------------LRTGKCVATLTG--------HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK------- 210

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 593 edpaqsagfhpsgsviAIGTLTGrwfvldtetkdlvtvHTDGneqLSVMRYSPDGNFLAIGSHDNYIYIYgvseNGRKYS 672
Cdd:cd00200  211 ----------------CLGTLRG---------------HENG---VNSVAFSPDGYLLASGSEDGTIRVW----DLRTGE 252

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 942127551 673 RIGKCSGHSSFITHLDWCVDSKHLISNSGDYEILYW 708
Cdd:cd00200  253 CVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
478-823 2.70e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 100.37  E-value: 2.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 478 LRDGTLVSGGGKDRKLISWTRNYQKICETEVPEQFGPVRTVAEGKGEVVLIGTTRNFVLQGTLSGDFHPITQGHTDELWG 557
Cdd:COG2319    4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 558 LAVHPVKAAFLTCGHDKHITLWDSTTHQPIWDKLI-EDPAQSAGFHPSGSVIAIGTLTGRWFVLDTETKDLVTVHTDGNE 636
Cdd:COG2319   84 VAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 637 QLSVMRYSPDGNFLAIGSHDNYIYIYGVsENGRKYSRIgkcSGHSSFITHLDWCVDSKHLISNSGDYEILYWissvckql 716
Cdd:COG2319  164 AVTSVAFSPDGKLLASGSDDGTVRLWDL-ATGKLLRTL---TGHTGAVRSVAFSPDGKLLASGSADGTVRLW-------- 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 717 vnvDITRGIEWAtytcTLGFHVFGVWpegsdgtdinAVCRS-QGKKLLSTGDDfGKVHLFSypcSQFRAPSHVYGGHSSH 795
Cdd:COG2319  232 ---DLATGKLLR----TLTGHSGSVR----------SVAFSpDGRLLASGSAD-GTVRLWD---LATGELLRTLTGHSGG 290

                        330       340
                 ....*....|....*....|....*...
gi 942127551 796 VTNVNFLYDDSHLIStGGKDMSIMQWRV 823
Cdd:COG2319  291 VNSVAFSPDGKLLAS-GSDDGTVRLWDL 317
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 20-74 2.56e-20

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: 85.04  E-value: 2.56e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 942127551  20 FCNDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQA 74
Cdd:cd21950    1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVA 55
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 549-822 4.45e-20

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 91.24  E-value: 4.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 549 QGHTDELWGLAVHPVKAAFLTCGHDKHITLWDSTTHQPIWdKLI--EDPAQSAGFHPSGSVIAIGTLTGRWFVLDTETKD 626
Cdd:cd00200   48 KGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVR-TLTghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 627 LVTV---HTDgneqlSVM--RYSPDGNFLAIGSHDNYIYIYgvseNGRKYSRIGKCSGHSSFITHLDWCVDSKHLISNSG 701
Cdd:cd00200  127 CLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLW----DLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 702 DYEILYWissvckqlvnvDITRGIEwatyTCTLGFHVFGVWpegsdgtdinAVCRSQGKKLLSTGDDFGKVHLFSypcSQ 781
Cdd:cd00200  198 DGTIKLW-----------DLSTGKC----LGTLRGHENGVN----------SVAFSPDGYLLASGSEDGTIRVWD---LR 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 942127551 782 FRAPSHVYGGHSSHVTNVNFLYDDSHLIStGGKDMSIMQWR 822
Cdd:cd00200  250 TGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 265-580 9.89e-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: 9.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 265 LYNVE-EQLQRHYTSHTDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRVWDSVSLNTLHVIGmGFFDrAVTCIAFS 343
Cdd:cd00200   35 VWDLEtGELLRTLKGHTGPVRDVAASADGTYLASG-----SSDKT-----IRLWDLETGECVRTLT-GHTS-YVSSVAFS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 344 KSngGSTLCAvdDSNDHILSVWDWQKEEKLADVKCSNEAVFAADFHPTDTnVIVTCGKSH-LYFWTLEGGSLNKkqgLFE 422
Cdd:cd00200  103 PD--GRILSS--SSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT-FVASSSQDGtIKLWDLRTGKCVA---TLT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 423 KQEKPkfVLCVTFSENGDT-ITGDSSGNILIWGKGTNRISYAIQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWtrnyq 501
Cdd:cd00200  175 GHTGE--VNSVAFSPDGEKlLSSSSDGTIKLWDLSTGKCLGTLRG-HENGVNSVAFSPDGYLLASGSEDGTIRVW----- 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942127551 502 kicetevpeqfgpvrtvaegkgevvligTTRNFVLQGTLsgdfhpitQGHTDELWGLAVHPVKAAFLTCGHDKHITLWD 580
Cdd:cd00200  247 ----------------------------DLRTGECVQTL--------SGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 32-79 1.34e-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: 79.87  E-value: 1.34e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 942127551  32 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 79
Cdd:cd21948    1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 32-74 1.28e-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: 76.81  E-value: 1.28e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 942127551  32 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQA 74
Cdd:cd21931    1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSS 43
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 28-72 1.14e-11

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: 60.04  E-value: 1.14e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 942127551  28 AASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQ 72
Cdd:cd21949    1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 549-821 3.35e-11

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: 65.05  E-value: 3.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 549 QGHTDELWGLAVHPVKAAFLTCGHDKHITLWDSTTHQPIwdkliedpaqsagfhpsgsviaiGTLTGrwfvldtetkdlv 628
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL-----------------------RTLKG------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 629 tvHTDGneqLSVMRYSPDGNFLAIGSHDNYIYIYgvseNGRKYSRIGKCSGHSSFITHLDWCVDSKHLISNSGDYEILYW 708
Cdd:cd00200   50 --HTGP---VRDVAASADGTYLASGSSDKTIRLW----DLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVW 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 709 issvckqlvnvditrgiEWATYTC--TLGFHvfgvwpegsdGTDINAVCRSQGKKLLSTGDDFGKVHLFSYPCSQFRaps 786
Cdd:cd00200  121 -----------------DVETGKCltTLRGH----------TDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCV--- 170

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 942127551 787 HVYGGHSSHVTNVNFLYDDSHLISTGGkDMSIMQW 821
Cdd:cd00200  171 ATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLW 204
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 679-824 7.50e-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: 54.65  E-value: 7.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551 679 GHSSFITHLDWCVDSKHLISNSGDYEILYWissvckqlvnvDITRGiewaTYTCTLGFHVFGVWpegsdgtdiNAVCRSQ 758
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW-----------DLETG----ELLRTLKGHTGPVR---------DVAASAD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942127551 759 GKKLLSTGDDfGKVHLFSYpcsQFRAPSHVYGGHSSHVTNVNFLyDDSHLISTGGKDMSIMQWRVI 824
Cdd:cd00200   63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 603-692 2.73e-04

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: 40.72  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942127551  603 PSGSVIAIGTLTGRWFVLDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNYIYIYGVsENGRKysrIGKCSGH 680
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDA-ENGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 942127551  681 SSFITHLDWCVD 692
Cdd:pfam12894  80 SDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 271-318 2.61e-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: 36.14  E-value: 2.61e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 942127551   271 QLQRHYTSHTDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRVWD 318
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
271-318 3.01e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 3.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 942127551  271 QLQRHYTSHTDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRVWD 318
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 549-580 7.00e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.98  E-value: 7.00e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 942127551   549 QGHTDELWGLAVHPVKAAFLTCGHDKHITLWD 580
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
549-580 9.73e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 9.73e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 942127551  549 QGHTDELWGLAVHPVKAAFLTCGHDKHITLWD 580
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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