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Conserved domains on  [gi|1958783789|ref|XP_038968475|]
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echinoderm microtubule-associated protein-like 1 isoform X2 [Rattus norvegicus]

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 ...
 191-262 3.19e-40

HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.


:

Pssm-ID: 460922  Cd Length: 72  Bit Score: 141.92  E-value: 3.19e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958783789 191 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 262
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
280-702 2.35e-30

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 124.25  E-value: 2.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 280 LAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGffDRAVTCIAFSKSNGGshlcAVDDSNDHVLSVW 359
Cdd:COG2319    32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFSPDGRL----LASASADGTVRLW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 360 DWQREERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTFSENGDTI-T 437
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAFSPDGKLLaS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 438 GDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgpirtVAEGKg 517
Cdd:COG2319   180 GSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD--------------------LATGK- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 518 nviligttrnfvLQGTLTGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIEDPAQSSGFH 596
Cdd:COG2319   238 ------------LLRTLTG--------HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 597 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRvgkcSGHSS 676
Cdd:COG2319   298 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL----TGHTG 373

                         410       420
                  ....*....|....*....|....*.
gi 1958783789 677 FITHLDWSVNSQFLVSNSGDYEILYW 702
Cdd:COG2319   374 AVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP-like super family cl41737
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 19-66 2.26e-28

trimerization domain of the echinoderm microtubule-associated protein-like family; The echinoderm microtubule-associated protein (EMAP)-like (EML) family includes EMAP-1, EMAP-2, EMAP-3, and EMAP-4. EMAP-1, also called EMAL1, EMAPL or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. EMAP-2, also called EML2 or EMAPL2, is a tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. EMAP-3, also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. EMAP-4, also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved trimerization domain located at the N-terminus of EML family members.


The actual alignment was detected with superfamily member cd21947:

Pssm-ID: 425368  Cd Length: 58  Bit Score: 107.88  E-value: 2.26e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958783789  19 MEISDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 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 ...
 673-818 8.31e-09

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: 57.73  E-value: 8.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 673 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVCRAH 752
Cdd:cd00200     7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958783789 753 EKKLLSTGDDfGKVHLFSYpcsQFRAPSHIYSGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 818
Cdd:cd00200    63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 191-262 3.19e-40

HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.


Pssm-ID: 460922  Cd Length: 72  Bit Score: 141.92  E-value: 3.19e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958783789 191 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 262
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
280-702 2.35e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 124.25  E-value: 2.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 280 LAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGffDRAVTCIAFSKSNGGshlcAVDDSNDHVLSVW 359
Cdd:COG2319    32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFSPDGRL----LASASADGTVRLW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 360 DWQREERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTFSENGDTI-T 437
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAFSPDGKLLaS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 438 GDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgpirtVAEGKg 517
Cdd:COG2319   180 GSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD--------------------LATGK- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 518 nviligttrnfvLQGTLTGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIEDPAQSSGFH 596
Cdd:COG2319   238 ------------LLRTLTG--------HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 597 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRvgkcSGHSS 676
Cdd:COG2319   298 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL----TGHTG 373

                         410       420
                  ....*....|....*....|....*.
gi 1958783789 677 FITHLDWSVNSQFLVSNSGDYEILYW 702
Cdd:COG2319   374 AVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 19-66 2.26e-28

trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm microtubule-associated protein-like 1 (EMAP-1), also called EMAL1, EMAPL, or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. This model corresponds to a conserved region located at the N-terminus of EMAP-1, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-4 and EMAP-2.


Pssm-ID: 409268  Cd Length: 58  Bit Score: 107.88  E-value: 2.26e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958783789  19 MEISDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 66
Cdd:cd21947    11 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 268-656 6.55e-26

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 108.58  E-value: 6.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 268 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 342
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 343 shLCAVddSNDHVLSVWDWQREERLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegnslnkkqglfekqekpk 422
Cdd:cd00200    66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 423 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKLhkaei 502
Cdd:cd00200   113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC----- 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 503 peqfgpirtvaegkgnviligttrnfvlQGTLTGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLWDA------- 575
Cdd:cd00200   170 ----------------------------VATLTG--------HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 576 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 653
Cdd:cd00200   214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                  ...
gi 1958783789 654 YIY 656
Cdd:cd00200   286 RIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 673-818 8.31e-09

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: 57.73  E-value: 8.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 673 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVCRAH 752
Cdd:cd00200     7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958783789 753 EKKLLSTGDDfGKVHLFSYpcsQFRAPSHIYSGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 818
Cdd:cd00200    63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 265-312 1.28e-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: 1.28e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958783789  265 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 312
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
265-312 1.33e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958783789 265 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 312
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 191-262 3.19e-40

HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.


Pssm-ID: 460922  Cd Length: 72  Bit Score: 141.92  E-value: 3.19e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958783789 191 KMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNV 262
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
280-702 2.35e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 124.25  E-value: 2.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 280 LAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGffDRAVTCIAFSKSNGGshlcAVDDSNDHVLSVW 359
Cdd:COG2319    32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--TAAVLSVAFSPDGRL----LASASADGTVRLW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 360 DWQREERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgLFEKQEKPKFVLCVTFSENGDTI-T 437
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKL-----LRTLTGHSGAVTSVAFSPDGKLLaS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 438 GDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqklhkaeipeqfgpirtVAEGKg 517
Cdd:COG2319   180 GSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWD--------------------LATGK- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 518 nviligttrnfvLQGTLTGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD-KIIEDPAQSSGFH 596
Cdd:COG2319   238 ------------LLRTLTG--------HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTlTGHSGGVNSVAFS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 597 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRvgkcSGHSS 676
Cdd:COG2319   298 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL----TGHTG 373

                         410       420
                  ....*....|....*....|....*.
gi 1958783789 677 FITHLDWSVNSQFLVSNSGDYEILYW 702
Cdd:COG2319   374 AVTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 19-66 2.26e-28

trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm microtubule-associated protein-like 1 (EMAP-1), also called EMAL1, EMAPL, or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. This model corresponds to a conserved region located at the N-terminus of EMAP-1, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-4 and EMAP-2.


Pssm-ID: 409268  Cd Length: 58  Bit Score: 107.88  E-value: 2.26e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958783789  19 MEISDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 66
Cdd:cd21947    11 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 268-656 6.55e-26

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 108.58  E-value: 6.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 268 RHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDS-----VTLNTLHVIGIgffdRAVTCIAFSKSngg 342
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLetgelLRTLKGHTGPV----RDVAASADGTY--- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 343 shLCAVddSNDHVLSVWDWQREERLADVKCSNEAVFAADFHPtDTNIIVTCGkshlyfwtlegnslnkkqglfekqekpk 422
Cdd:cd00200    66 --LASG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSS---------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 423 fvlcvtfsengdtitgdSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKLhkaei 502
Cdd:cd00200   113 -----------------RDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC----- 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 503 peqfgpirtvaegkgnviligttrnfvlQGTLTGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLWDA------- 575
Cdd:cd00200   170 ----------------------------VATLTG--------HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLstgkclg 213

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 576 --VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCI 653
Cdd:cd00200   214 tlRGH--------ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTI 285


                  ...
gi 1958783789 654 YIY 656
Cdd:cd00200   286 RIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
257-660 1.58e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.00  E-value: 1.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 257 VVLYNVE-EQLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDSVTLNTLHVIGIGffDRAVTCIA 335
Cdd:COG2319   102 VRLWDLAtGLLLRTLTGHTGAVRSVAFSPDGKTLASG-----SADGT-----VRLWDLATGKLLRTLTGH--SGAVTSVA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 336 FSKSngGSHLcaVDDSNDHVLSVWDWQREERLADVKCSNEAVFAADFHPtDTNIIVTCGKSH-LYFWTLEGNSLnkkqgL 414
Cdd:COG2319   170 FSPD--GKLL--ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATGKL-----L 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 415 FEKQEKPKFVLCVTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgn 493
Cdd:COG2319   240 RTLTGHSGSVRSVAFSPDGRLLaSGSADGTVRLWDLATGELLRTLTG-HSGGVNSVAFSPDGKLLASGSDDGTVRLWD-- 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 494 yqklhkaeipeqfgpirtVAEGKgnviligttrnfvLQGTLTGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLW 573
Cdd:COG2319   317 ------------------LATGK-------------LLRTLTG--------HTGAVRSVAFSPDGKTLASGSDDGTVRLW 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 574 DAVGHRPVwdkiiedpaqssgfhpsgsvvavGTLTGrwfvfdtetkdlvtvHTDGneqLSVMRYSPDGNFLAIGSHDNCI 653
Cdd:COG2319   358 DLATGELL-----------------------RTLTG---------------HTGA---VTSVAFSPDGRTLASGSADGTV 396


                  ....*..
gi 1958783789 654 YIYGVSD 660
Cdd:COG2319   397 RLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
347-817 2.20e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 106.53  E-value: 2.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 347 AVDDSNDHVLSVWDWQREERLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGNSLnkkqgLFEKQEKPKFVLC 426
Cdd:COG2319     9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGAL-----LATLLGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 427 VTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDG-TLVSGGGkDRRLISWNgnyqklhkaeipe 504
Cdd:COG2319    84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSA-DGTVRLWD------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 505 qfgpirtVAEGKgnviligttrnfvLQGTLTGdftpitqgHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWD- 583
Cdd:COG2319   149 -------LATGK-------------LLRTLTG--------HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 584 KIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGR 663
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 664 KYTRvgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvSVETTRDIEwatytcTLGFHVFGVWpegsdgt 743
Cdd:COG2319   281 LRTL----TGHSGGVNSVAFSPDGKLLASGSDDGTVRLW---------DLATGKLLR------TLTGHTGAVR------- 334

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958783789 744 dinAVCRAHEKKLLSTGDDFGKVHLFSypcSQFRAPSHIYSGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 817
Cdd:COG2319   335 ---SVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFS-PDGRTLASGSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
472-817 3.11e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 96.90  E-value: 3.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 472 LRDGTLVSGGGKDRRLISWNGNYQKLHKAEIPEQFGPIRTVAEGKGNVILIGTTRNFVLQGTLTGDFTPITQGHTDELWG 551
Cdd:COG2319     4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 552 LAIHASKPQFLTCGHDKHATLWDAV-GHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNE 630
Cdd:COG2319    84 VAFSPDGRLLASASADGTVRLWDLAtGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 631 QLSVMRYSPDGNFLAIGSHDNCIYIYGVsDNGRKYTRVgkcSGHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqv 710
Cdd:COG2319   164 AVTSVAFSPDGKLLASGSDDGTVRLWDL-ATGKLLRTL---TGHTGAVRSVAFSPDGKLLASGSADGTVRLW-------- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 711 vSVETTRDIewatytCTLGFHVFGVW-----PEGsdgtdinavcraheKKLLSTGDDfGKVHLFSypcSQFRAPSHIYSG 785
Cdd:COG2319   232 -DLATGKLL------RTLTGHSGSVRsvafsPDG--------------RLLASGSAD-GTVRLWD---LATGELLRTLTG 286

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1958783789 786 HSSHVTNVDFLcEDSHLISTGGKDTSIMQWRV 817
Cdd:COG2319   287 HSGGVNSVAFS-PDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 462-816 1.96e-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: 92.40  E-value: 1.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 462 HEGGIFALCMLRDG-TLVSGGGkDRRLISWNgnyqklhkaeipeqfgpirtvaegkgnviligtTRNFVLQGTLTGdftp 540
Cdd:cd00200     8 HTGGVTCVAFSPDGkLLATGSG-DGTIKVWD---------------------------------LETGELLRTLKG---- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 541 itqgHTDELWGLAIHASKPQFLTCGHDKHATLWDA---------VGHR-PVWdkiiedpaqSSGFHPSGSVVAVGTLTGR 610
Cdd:cd00200    50 ----HTGPVRDVAASADGTYLASGSSDKTIRLWDLetgecvrtlTGHTsYVS---------SVAFSPDGRILSSSSRDKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 611 WFVFDTETKDLVTV---HTDgneqlSVM--RYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTrvgkCSGHSSFITHLDWSV 685
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDLRTGKCVAT----LTGHTGEVNSVAFSP 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 686 NSQFLVSNSGDYEILYWVPSACKQVvsvettrdiewatytCTLGFHVFGVWpegsdgtdinAVCRAHEKKLLSTGDDFGK 765
Cdd:cd00200   188 DGEKLLSSSSDGTIKLWDLSTGKCL---------------GTLRGHENGVN----------SVAFSPDGYLLASGSEDGT 242

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958783789 766 VHLFSypcSQFRAPSHIYSGHSSHVTNVDFlCEDSHLISTGGKDTSIMQWR 816
Cdd:cd00200   243 IRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 259-574 1.64e-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: 89.70  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 259 LYNVE-EQLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWDSVTLNTLHVIGiGFFDrAVTCIAFS 337
Cdd:cd00200    35 VWDLEtGELLRTLKGHTGPVRDVAASADGTYLASG-----SSDKT-----IRLWDLETGECVRTLT-GHTS-YVSSVAFS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 338 KSNggsHLcAVDDSNDHVLSVWDWQREERLADVKCSNEAVFAADFHPTDTnIIVTCGKSH-LYFWTLEGNSLNKkqgLFE 416
Cdd:cd00200   103 PDG---RI-LSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT-FVASSSQDGtIKLWDLRTGKCVA---TLT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 417 KQEKPkfVLCVTFSENGDT-ITGDSSGNILVWGKGTnRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyq 495
Cdd:cd00200   175 GHTGE--VNSVAFSPDGEKlLSSSSDGTIKLWDLST-GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD---- 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958783789 496 klhkaeipeqfgpirtvaegkgnviligtTRNFVLQGTLtgdftpitQGHTDELWGLAIHASKPQFLTCGHDKHATLWD 574
Cdd:cd00200   248 -----------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 418-702 4.12e-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: 4.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 418 QEKPKFVLCVTFSENGDTI-TGDSSGNILVWGKGTNRISYAVQGaHEGGIFALCMLRDGTLVSGGGKDRRLISWNgnyqk 496
Cdd:cd00200     6 KGHTGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWD----- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 497 lhkaeiPEQFGPIRTVAegkgnviligttrnfvlqgtltgdftpitqGHTDELWGLAIHASKPQFLTCGHDKHATLWDAV 576
Cdd:cd00200    80 ------LETGECVRTLT------------------------------GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 577 ---------GHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIG 647
Cdd:cd00200   124 tgkclttlrGH--------TDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSS 195

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958783789 648 SHDNCIYIYGVSDnGRKytrVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYW 702
Cdd:cd00200   196 SSDGTIKLWDLST-GKC---LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 19-66 5.37e-18

trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm microtubule-associated protein-like 2 (EMAP-2), also called EML2 or EMAPL2, is a tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. This model corresponds to the N-terminal trimerization domain of EMAP-2.


Pssm-ID: 409269  Cd Length: 48  Bit Score: 77.94  E-value: 5.37e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958783789  19 MEISDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRK 66
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 19-62 1.23e-16

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: 74.11  E-value: 1.23e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958783789  19 MEISDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAV 62
Cdd:cd21931     1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 543-817 4.50e-16

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: 79.69  E-value: 4.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 543 QGHTDELWGLAIHASKPQFLTCGHDKHATLWDA---------VGHrpvwdkiiEDPAQSSGFHPSGSVVAVGTLTGRWFV 613
Cdd:cd00200     6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLetgellrtlKGH--------TGPVRDVAASADGTYLASGSSDKTIRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 614 FDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTrvgkCSGHSSFITHLDWSVNSQFLVSN 693
Cdd:cd00200    78 WDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT----LRGHTDWVNSVAFSPDGTFVASS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 694 SGDYEILYWVPSACKQVvsvettrdiewatytctlgfHVFgvwpEGSDGtDINAVC-RAHEKKLLSTGDDfGKVHLFSYP 772
Cdd:cd00200   154 SQDGTIKLWDLRTGKCV--------------------ATL----TGHTG-EVNSVAfSPDGEKLLSSSSD-GTIKLWDLS 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1958783789 773 CSQFrapSHIYSGHSSHVTNVDFlCEDSHLISTGGKDTSIMQWRV 817
Cdd:cd00200   208 TGKC---LGTLRGHENGVNSVAF-SPDGYLLASGSEDGTIRVWDL 248
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 20-61 5.33e-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: 64.24  E-value: 5.33e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958783789  20 EISDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQA 61
Cdd:cd21950    14 DVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVA 55
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 23-59 2.69e-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: 2.69e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958783789  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 ...
 673-818 8.31e-09

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: 57.73  E-value: 8.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 673 GHSSFITHLDWSVNSQFLVSNSGDYEILYWvpsackqvvsvettrDIEWATYTCTLGFHVFGVWpegsdgtdiNAVCRAH 752
Cdd:cd00200     7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVW---------------DLETGELLRTLKGHTGPVR---------DVAASAD 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958783789 753 EKKLLSTGDDfGKVHLFSYpcsQFRAPSHIYSGHSSHVTNVDFLcEDSHLISTGGKDTSIMQWRVI 818
Cdd:cd00200    63 GTYLASGSSD-KTIRLWDL---ETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 265-312 1.28e-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: 1.28e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958783789  265 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGKqlpphVRIWD 312
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
265-312 1.33e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958783789 265 QLQRHYAGHNDDVKCLAVHPDRITIATGqvagtSKDGkqlppHVRIWD 312
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 597-686 2.72e-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: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958783789 597 PSGSVVAVGTLTGRWFVFDTETKDLVTVHTDgNEQLSV--MRYSPDGNFLAIGSHDNCIYIYGVSdNGRKytrVGKCSGH 674
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLDAE-NGKI---VHHFSAG 79

                          90
                  ....*....|..
gi 1958783789 675 SSFITHLDWSVN 686
Cdd:pfam12894  80 SDLITCLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 543-574 9.34e-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: 9.34e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958783789  543 QGHTDELWGLAIHASKPQFLTCGHDKHATLWD 574
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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