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Conserved domains on  [gi|966956603|ref|XP_014999957|]
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echinoderm microtubule-associated protein-like 1 isoform X2 [Macaca mulatta]

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 ...
 213-284 6.56e-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: 6.56e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966956603  213 KMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 284
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
369-724 3.28e-30

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.87  E-value: 3.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 369 AVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLnkkqgLFEKQEKPKFVLC 448
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL-----LRTLTGHTGAVRS 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 449 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTeIPEQ 527
Cdd:COG2319  126 VAFSPDGKTLaSGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 528 FGPIRTVA---EGKgdVILIGTTRNFVLQGTL-SGDFTPITQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPV 603
Cdd:COG2319  204 TGAVRSVAfspDGK--LLASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELL 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 604 WD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSD 682
Cdd:COG2319  282 RTlTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 966956603 683 NGRKYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 724
Cdd:COG2319  362 GELLRTL----TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 19-66 3.07e-29

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: 110.58  E-value: 3.07e-29
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 966956603  19 MEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 66
Cdd:cd21947   11 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 695-840 1.47e-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: 56.96  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 695 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVSRAH 774
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966956603 775 EKKLLSTGDDfGKVHLFSYpcsQFRAPSHIYGGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 840
Cdd:cd00200   63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 287-334 1.20e-03

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


:

Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.29  E-value: 1.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 966956603   287 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 334
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 ...
 213-284 6.56e-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: 6.56e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966956603  213 KMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 284
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
369-724 3.28e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.87  E-value: 3.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 369 AVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLnkkqgLFEKQEKPKFVLC 448
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL-----LRTLTGHTGAVRS 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 449 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTeIPEQ 527
Cdd:COG2319  126 VAFSPDGKTLaSGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 528 FGPIRTVA---EGKgdVILIGTTRNFVLQGTL-SGDFTPITQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPV 603
Cdd:COG2319  204 TGAVRSVAfspDGK--LLASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELL 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 604 WD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSD 682
Cdd:COG2319  282 RTlTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 966956603 683 NGRKYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 724
Cdd:COG2319  362 GELLRTL----TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 19-66 3.07e-29

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: 110.58  E-value: 3.07e-29
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 966956603  19 MEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 66
Cdd:cd21947   11 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 290-678 1.39e-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: 113.58  E-value: 1.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 290 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 364
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 365 tnLCAVddSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegsslnkkqglfekqekpk 444
Cdd:cd00200   66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 445 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTei 524
Cdd:cd00200  113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVAT-- 172

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 525 peqfgpirtvaegkgdviligttrnfvlqgtlsgdFTpitqGHTDELWGLAIHASKPQFLTCGHDKHATLWDA------- 597
Cdd:cd00200  173 -----------------------------------LT----GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 598 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 675
Cdd:cd00200  214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                 ...
gi 966956603 676 YIY 678
Cdd:cd00200  286 RIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 695-840 1.47e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 56.96  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 695 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVSRAH 774
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966956603 775 EKKLLSTGDDfGKVHLFSYpcsQFRAPSHIYGGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 840
Cdd:cd00200   63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 287-334 1.20e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.29  E-value: 1.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 966956603   287 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 334
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
287-334 1.32e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966956603  287 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 334
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 619-708 3.11e-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: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603  619 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNCIYIYGVSdNGRKytrVGKCSGH 696
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDAE-NGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 966956603  697 SSFITHLDWSVN 708
Cdd:pfam12894  80 SDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 565-596 9.41e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.60  E-value: 9.41e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 966956603   565 QGHTDELWGLAIHASKPQFLTCGHDKHATLWD 596
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 ...
 213-284 6.56e-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: 6.56e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966956603  213 KMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 284
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
369-724 3.28e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.87  E-value: 3.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 369 AVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLnkkqgLFEKQEKPKFVLC 448
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL-----LRTLTGHTGAVRS 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 449 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTeIPEQ 527
Cdd:COG2319  126 VAFSPDGKTLaSGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 528 FGPIRTVA---EGKgdVILIGTTRNFVLQGTL-SGDFTPITQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPV 603
Cdd:COG2319  204 TGAVRSVAfspDGK--LLASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELL 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 604 WD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSD 682
Cdd:COG2319  282 RTlTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 966956603 683 NGRKYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 724
Cdd:COG2319  362 GELLRTL----TGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 19-66 3.07e-29

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: 110.58  E-value: 3.07e-29
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 966956603  19 MEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 66
Cdd:cd21947   11 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 290-678 1.39e-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: 113.58  E-value: 1.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 290 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 364
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 365 tnLCAVddSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegsslnkkqglfekqekpk 444
Cdd:cd00200   66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 445 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTei 524
Cdd:cd00200  113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVAT-- 172

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 525 peqfgpirtvaegkgdviligttrnfvlqgtlsgdFTpitqGHTDELWGLAIHASKPQFLTCGHDKHATLWDA------- 597
Cdd:cd00200  173 -----------------------------------LT----GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 598 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 675
Cdd:cd00200  214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                 ...
gi 966956603 676 YIY 678
Cdd:cd00200  286 RIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
278-682 3.10e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.23  E-value: 3.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 278 VVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTskdgkqlpphVRIWDSVTLNTLHVIGIgfFDRAVTCIA 357
Cdd:COG2319   60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT----------VRLWDLATGLLLRTLTG--HTGAVRSVA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 358 FSkSNGGTNLCAvddSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGSSLnkkqgL 436
Cdd:COG2319  128 FS-PDGKTLASG---SADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGtVRLWDLATGKL-----L 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 437 FEKQEKPKFVLCVTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSgn 515
Cdd:COG2319  198 RTLTGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTG-HSGSVRSVAFSPDGRLLASGSADGTVRLWD-- 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 516 yqklrkteipeqfgpirtVAEGKgdviligttrnfvLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLW 595
Cdd:COG2319  275 ------------------LATGE-------------LLRTL--------TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 596 DAVGHRPVWD-KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNC 674
Cdd:COG2319  316 DLATGKLLRTlTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395


                 ....*...
gi 966956603 675 IYIYGVSD 682
Cdd:COG2319  396 VRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
369-839 1.79e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.84  E-value: 1.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 369 AVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLnkkqgLFEKQEKPKFVLC 448
Cdd:COG2319    9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL-----LATLLGHTAAVLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 449 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDG-TLVSGGGkDRKLISWSgnyqklrkteipe 526
Cdd:COG2319   84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSA-DGTVRLWD------------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 527 qfgpirtVAEGKgdviligttrnfvLQGTLSGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD- 605
Cdd:COG2319  149 -------LATGK-------------LLRTLTG--------HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 606 KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGR 685
Cdd:COG2319  201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 686 KYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvSVETTRDIEwatytcTLGFHVFGVWpegsdgt 765
Cdd:COG2319  281 LRTL----TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW---------DLATGKLLR------TLTGHTGAVR------- 334

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966956603 766 dinAVSRAHEKKLLSTGDDFGKVHLFSypcSQFRAPSHIYGGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 839
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 ...
 281-596 7.80e-20

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 90.86  E-value: 7.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 281 LYNVE-EQLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDSVTLNTLHVIGiGFFDrAVTCIAFS 359
Cdd:cd00200   35 VWDLEtGELLRTLKGHTGPVRDVAASADGTYLASG-----SSDKT-----IRLWDLETGECVRTLT-GHTS-YVSSVAFS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 360 KSNGgtnlCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTnIIVTCGKSH-LYFWTLEGSSLNKkqgLFE 438
Cdd:cd00200  103 PDGR----ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT-FVASSSQDGtIKLWDLRTGKCVA---TLT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 439 KQEKPkfVLCVTFSENGDT-ITGDSSGNILVWGKGTnRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRKLISWSgnyq 517
Cdd:cd00200  175 GHTGE--VNSVAFSPDGEKlLSSSSDGTIKLWDLST-GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD---- 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966956603 518 klrkteipeqfgpirtvaegkgdviligtTRNFVLQGTLsgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWD 596
Cdd:cd00200  248 -----------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 440-724 4.69e-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: 88.55  E-value: 4.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 440 QEKPKFVLCVTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRKLISWSgnyqk 518
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWD----- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 519 lrkteiPEQFGPIRTVAegkgdviligttrnfvlqgtlsgdftpitqGHTDELWGLAIHASKPQFLTCGHDKHATLWDAV 598
Cdd:cd00200   80 ------LETGECVRTLT------------------------------GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 599 ---------GHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIG 669
Cdd:cd00200  124 tgkclttlrGH--------TDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSS 195

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 966956603 670 SHDNCIYIYGVSDnGRKytrVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 724
Cdd:cd00200  196 SSDGTIKLWDLST-GKC---LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 19-66 2.93e-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: 2.93e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 966956603  19 MEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 66
Cdd:cd21948    1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 19-62 7.84e-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: 7.84e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 966956603  19 MEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAV 62
Cdd:cd21931    1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 565-839 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 966956603 565 QGHTDELWGLAIHASKPQFLTCGHDKHATLWDA---------VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFV 635
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLetgellrtlKGH--------TGPVRDVAASADGTYLASGSSDKTIRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 636 FDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTrvgkCSGHSSFITHLDWSVNSQFLVSN 715
Cdd:cd00200   78 WDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT----LRGHTDWVNSVAFSPDGTFVASS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 716 SGDYEILYWVPSACKQVvsvettrdiewatytctlgfHVFgvwpEGSDGtDINAVS-RAHEKKLLSTGDDfGKVHLFSYP 794
Cdd:cd00200  154 SQDGTIKLWDLRTGKCV--------------------ATL----TGHTG-EVNSVAfSPDGEKLLSSSSD-GTIKLWDLS 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 966956603 795 CSQFrapSHIYGGHSSHVTNVDFlCEDSHLISTGGKDTSIMQWRV 839
Cdd:cd00200  208 TGKC---LGTLRGHENGVNSVAF-SPDGYLLASGSEDGTIRVWDL 248
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 20-61 2.56e-13

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


Pssm-ID: 409271  Cd Length: 59  Bit Score: 65.39  E-value: 2.56e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 966956603  20 EVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQA 61
Cdd:cd21950   14 DVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVA 55
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 23-59 2.76e-10

trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm microtubule-associated protein-like 3 (EMAP-3), also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. It may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved region located at the N-terminus of EMAP-3, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-2 and EMAP-4.


Pssm-ID: 409270  Cd Length: 48  Bit Score: 56.18  E-value: 2.76e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 966956603  23 DRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQ 59
Cdd:cd21949    9 DPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 695-840 1.47e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 56.96  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603 695 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVSRAH 774
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966956603 775 EKKLLSTGDDfGKVHLFSYpcsQFRAPSHIYGGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 840
Cdd:cd00200   63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 287-334 1.20e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.29  E-value: 1.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 966956603   287 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 334
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
287-334 1.32e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966956603  287 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 334
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 619-708 3.11e-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: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966956603  619 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNCIYIYGVSdNGRKytrVGKCSGH 696
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDAE-NGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 966956603  697 SSFITHLDWSVN 708
Cdd:pfam12894  80 SDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 565-596 9.41e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.60  E-value: 9.41e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 966956603   565 QGHTDELWGLAIHASKPQFLTCGHDKHATLWD 596
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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