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Conserved domains on  [gi|254763417|sp|O00423|]
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RecName: Full=Echinoderm microtubule-associated protein-like 1; Short=EMAP-1; Short=HuEMAP-1

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 ...
 188-259 6.21e-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: 141.15  E-value: 6.21e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254763417  188 KMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 259
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 22-79 8.77e-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: 131.77  E-value: 8.77e-37
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254763417  22 NDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 79
Cdd:cd21947    1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
344-699 3.55e-30

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.87  E-value: 3.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 344 AVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLnkkqgLFEKQEKPKFVLC 423
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL-----LRTLTGHTGAVRS 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 424 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTeIPEQ 502
Cdd:COG2319  126 VAFSPDGKTLaSGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 503 FGPIRTVA---EGKgdVILIGTTRNFVLQGTL-SGDFTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPV 578
Cdd:COG2319  204 TGAVRSVAfspDGK--LLASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELL 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 579 WD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSD 657
Cdd:COG2319  282 RTlTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 254763417 658 NGRKYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 699
Cdd:COG2319  362 GELLRTL----TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 670-815 1.05e-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: 57.34  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 670 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVCRAH 749
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254763417 750 EKKLLSTGDDfGKVHLFSYpcsQFRAPSHIYGGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 815
Cdd:cd00200   63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 262-309 1.55e-03

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


:

Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 36.91  E-value: 1.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 254763417   262 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 309
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 ...
 188-259 6.21e-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: 141.15  E-value: 6.21e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254763417  188 KMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 259
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 22-79 8.77e-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: 131.77  E-value: 8.77e-37
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254763417  22 NDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 79
Cdd:cd21947    1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
344-699 3.55e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.87  E-value: 3.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 344 AVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLnkkqgLFEKQEKPKFVLC 423
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL-----LRTLTGHTGAVRS 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 424 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTeIPEQ 502
Cdd:COG2319  126 VAFSPDGKTLaSGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 503 FGPIRTVA---EGKgdVILIGTTRNFVLQGTL-SGDFTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPV 578
Cdd:COG2319  204 TGAVRSVAfspDGK--LLASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELL 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 579 WD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSD 657
Cdd:COG2319  282 RTlTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 254763417 658 NGRKYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 699
Cdd:COG2319  362 GELLRTL----TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 265-653 1.97e-27

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: 112.81  E-value: 1.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 265 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 339
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 340 tnLCAVddSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegsslnkkqglfekqekpk 419
Cdd:cd00200   66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 420 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTei 499
Cdd:cd00200  113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVAT-- 172

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 500 peqfgpirtvaegkgdviligttrnfvlqgtlsgdFTpitqGHTDELWGLAIHASKSQFLTCGHDKHATLWDA------- 572
Cdd:cd00200  173 -----------------------------------LT----GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 573 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 650
Cdd:cd00200  214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                 ...
gi 254763417 651 YIY 653
Cdd:cd00200  286 RIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 670-815 1.05e-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: 57.34  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 670 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVCRAH 749
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254763417 750 EKKLLSTGDDfGKVHLFSYpcsQFRAPSHIYGGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 815
Cdd:cd00200   63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 262-309 1.55e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 36.91  E-value: 1.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 254763417   262 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 309
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
262-309 1.65e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 254763417  262 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 309
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 594-683 2.87e-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: 37.64  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417  594 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNCIYIYGVSdNGRKytrVGKCSGH 671
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDAE-NGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 254763417  672 SSFITHLDWSVN 683
Cdd:pfam12894  80 SDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 540-571 6.99e-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: 6.99e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 254763417   540 QGHTDELWGLAIHASKSQFLTCGHDKHATLWD 571
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 ...
 188-259 6.21e-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: 141.15  E-value: 6.21e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254763417  188 KMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 259
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 22-79 8.77e-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: 131.77  E-value: 8.77e-37
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254763417  22 NDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 79
Cdd:cd21947    1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
344-699 3.55e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.87  E-value: 3.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 344 AVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLnkkqgLFEKQEKPKFVLC 423
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL-----LRTLTGHTGAVRS 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 424 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTeIPEQ 502
Cdd:COG2319  126 VAFSPDGKTLaSGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 503 FGPIRTVA---EGKgdVILIGTTRNFVLQGTL-SGDFTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPV 578
Cdd:COG2319  204 TGAVRSVAfspDGK--LLASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELL 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 579 WD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSD 657
Cdd:COG2319  282 RTlTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 254763417 658 NGRKYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 699
Cdd:COG2319  362 GELLRTL----TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 265-653 1.97e-27

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: 112.81  E-value: 1.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 265 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 339
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 340 tnLCAVddSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegsslnkkqglfekqekpk 419
Cdd:cd00200   66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 420 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTei 499
Cdd:cd00200  113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVAT-- 172

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 500 peqfgpirtvaegkgdviligttrnfvlqgtlsgdFTpitqGHTDELWGLAIHASKSQFLTCGHDKHATLWDA------- 572
Cdd:cd00200  173 -----------------------------------LT----GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 573 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 650
Cdd:cd00200  214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                 ...
gi 254763417 651 YIY 653
Cdd:cd00200  286 RIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
253-657 2.52e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.23  E-value: 2.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 253 VVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTskdgkqlpphVRIWDSVTLNTLHVIGIgfFDRAVTCIA 332
Cdd:COG2319   60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT----------VRLWDLATGLLLRTLTG--HTGAVRSVA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 333 FSkSNGGTNLCAvddSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGSSLnkkqgL 411
Cdd:COG2319  128 FS-PDGKTLASG---SADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGtVRLWDLATGKL-----L 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 412 FEKQEKPKFVLCVTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSgn 490
Cdd:COG2319  198 RTLTGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTG-HSGSVRSVAFSPDGRLLASGSADGTVRLWD-- 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 491 yqklrkteipeqfgpirtVAEGKgdviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKSQFLTCGHDKHATLW 570
Cdd:COG2319  275 ------------------LATGE-------------LLRTL--------TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 571 DAVGHRPVWD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNC 649
Cdd:COG2319  316 DLATGKLLRTlTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395


                 ....*...
gi 254763417 650 IYIYGVSD 657
Cdd:COG2319  396 VRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
344-814 1.14e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.22  E-value: 1.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 344 AVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLnkkqgLFEKQEKPKFVLC 423
Cdd:COG2319    9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL-----LATLLGHTAAVLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 424 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDG-TLVSGGGkDRKLISWSgnyqklrkteipe 501
Cdd:COG2319   84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSA-DGTVRLWD------------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 502 qfgpirtVAEGKgdviligttrnfvLQGTLSGdftpitqgHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPVWD- 580
Cdd:COG2319  149 -------LATGK-------------LLRTLTG--------HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 581 KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGR 660
Cdd:COG2319  201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 661 KYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvSVETTRDIEwatytcTLGFHVFGVWpegsdgt 740
Cdd:COG2319  281 LRTL----TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW---------DLATGKLLR------TLTGHTGAVR------- 334

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254763417 741 dinAVCRAHEKKLLSTGDDFGKVHLFSypcSQFRAPSHIYGGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 814
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 ...
 256-571 2.07e-19

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: 89.32  E-value: 2.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 256 LYNVE-EQLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDSVTLNTLHVIGiGFFDrAVTCIAFS 334
Cdd:cd00200   35 VWDLEtGELLRTLKGHTGPVRDVAASADGTYLASG-----SSDKT-----IRLWDLETGECVRTLT-GHTS-YVSSVAFS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 335 KSNGgtnlCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTnIIVTCGKSH-LYFWTLEGSSLNKkqgLFE 413
Cdd:cd00200  103 PDGR----ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT-FVASSSQDGtIKLWDLRTGKCVA---TLT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 414 KQEKPkfVLCVTFSENGDT-ITGDSSGNILVWGKGTnRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRKLISWSgnyq 492
Cdd:cd00200  175 GHTGE--VNSVAFSPDGEKlLSSSSDGTIKLWDLST-GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD---- 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254763417 493 klrkteipeqfgpirtvaegkgdviligtTRNFVLQGTLsgdftpitQGHTDELWGLAIHASKSQFLTCGHDKHATLWD 571
Cdd:cd00200  248 -----------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 20-74 4.79e-19

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: 81.57  E-value: 4.79e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254763417  20 FCNDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQA 74
Cdd:cd21950    1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVA 55
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 415-699 9.63e-19

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: 87.39  E-value: 9.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 415 QEKPKFVLCVTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSgnyqk 493
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWD----- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 494 lrkteiPEQFGPIRTVAegkgdviligttrnfvlqgtlsgdftpitqGHTDELWGLAIHASKSQFLTCGHDKHATLWDAV 573
Cdd:cd00200   80 ------LETGECVRTLT------------------------------GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 574 ---------GHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIG 644
Cdd:cd00200  124 tgkclttlrGH--------TDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSS 195

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254763417 645 SHDNCIYIYGVSDnGRKytrVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 699
Cdd:cd00200  196 SSDGTIKLWDLST-GKC---LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 32-79 2.84e-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: 78.71  E-value: 2.84e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 254763417  32 MEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 79
Cdd:cd21948    1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 32-75 7.61e-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: 74.50  E-value: 7.61e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 254763417  32 MEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAV 75
Cdd:cd21931    1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 540-814 2.16e-15

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: 77.38  E-value: 2.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 540 QGHTDELWGLAIHASKSQFLTCGHDKHATLWDA---------VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFV 610
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLetgellrtlKGH--------TGPVRDVAASADGTYLASGSSDKTIRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 611 FDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTrvgkCSGHSSFITHLDWSVNSQFLVSN 690
Cdd:cd00200   78 WDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT----LRGHTDWVNSVAFSPDGTFVASS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 691 SGDYEILYWVPSACKQVvsvettrdiewatytctlgfHVFgvwpEGSDGtDINAVC-RAHEKKLLSTGDDfGKVHLFSYP 769
Cdd:cd00200  154 SQDGTIKLWDLRTGKCV--------------------ATL----TGHTG-EVNSVAfSPDGEKLLSSSSD-GTIKLWDLS 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 254763417 770 CSQFrapSHIYGGHSSHVTNVDFlCEDSHLISTGGKDTSIMQWRV 814
Cdd:cd00200  208 TGKC---LGTLRGHENGVNSVAF-SPDGYLLASGSEDGTIRVWDL 248
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 28-72 1.03e-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: 1.03e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 254763417  28 AASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQ 72
Cdd:cd21949    1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 670-815 1.05e-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: 57.34  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417 670 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVCRAH 749
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254763417 750 EKKLLSTGDDfGKVHLFSYpcsQFRAPSHIYGGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 815
Cdd:cd00200   63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 262-309 1.55e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 36.91  E-value: 1.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 254763417   262 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 309
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
262-309 1.65e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 254763417  262 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 309
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 594-683 2.87e-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: 37.64  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254763417  594 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNCIYIYGVSdNGRKytrVGKCSGH 671
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDAE-NGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 254763417  672 SSFITHLDWSVN 683
Cdd:pfam12894  80 SDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 540-571 6.99e-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: 6.99e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 254763417   540 QGHTDELWGLAIHASKSQFLTCGHDKHATLWD 571
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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