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Conserved domains on  [gi|1207128528|ref|XP_021322905|]
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echinoderm microtubule-associated protein-like 1 isoform X4 [Danio rerio]

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 ...
 205-276 9.61e-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: 140.77  E-value: 9.61e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207128528 205 KMYLKGRPITMYMPKDLVDTYCLETKADLPPKKLKLDWVYGYRGRDCRSNLYLLPTGETVYFIASVVVLYNV 276
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 22-79 4.17e-37

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


:

Pssm-ID: 409268  Cd Length: 58  Bit Score: 132.92  E-value: 4.17e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207128528  22 NDDSASATSSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNKK 79
Cdd:cd21947     1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
361-715 1.02e-34

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 137.35  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 361 VVDDSNDHMLSVWDWQREDRLAEVKCSNESVFAADFHPTDANIIVTCGKSHLCFWSLEKGSLvkkqgLFEKQEKPKFVLC 440
Cdd:COG2319    51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL-----LRTLTGHTGAVRS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 441 VTFSENGDAI-TGDSSGNILVWGKGSNRISLAIQGaHEASVFALCMLRNG-TLVSGGKDRKLISWD-ENFQKIQTVEVPE 517
Cdd:COG2319   126 VAFSPDGKTLaSGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGkLLASGSDDGTVRLWDlATGKLLRTLTGHT 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 518 lyGPVRTVAEGR-GETVLIGTTKNYVLQGSLN-GEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHIYLWDSDSHQPIW 595
Cdd:COG2319   205 --GAVRSVAFSPdGKLLASGSADGTVRLWDLAtGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 596 TKT-LEDSAQSAGFHPSGATVAVGMQTGRWLVLDTESKDLVTVHTDGNEQLSVIRFSPDGNFLAIGSHDNYIYIYAVAEN 674
Cdd:COG2319   283 TLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1207128528 675 GkkysRVGKCSGHSSFITHLDWSVDSQYLVSNSGDYEILYW 715
Cdd:COG2319   363 E----LLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 279-326 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 1207128528  279 QLQRHYTGHTDDIKCLAVHPDKITIATGqvagtSSDGKqlaphVRVWD 326
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 ...
 205-276 9.61e-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: 140.77  E-value: 9.61e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207128528 205 KMYLKGRPITMYMPKDLVDTYCLETKADLPPKKLKLDWVYGYRGRDCRSNLYLLPTGETVYFIASVVVLYNV 276
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 22-79 4.17e-37

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


Pssm-ID: 409268  Cd Length: 58  Bit Score: 132.92  E-value: 4.17e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207128528  22 NDDSASATSSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNKK 79
Cdd:cd21947     1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
361-715 1.02e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 137.35  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 361 VVDDSNDHMLSVWDWQREDRLAEVKCSNESVFAADFHPTDANIIVTCGKSHLCFWSLEKGSLvkkqgLFEKQEKPKFVLC 440
Cdd:COG2319    51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL-----LRTLTGHTGAVRS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 441 VTFSENGDAI-TGDSSGNILVWGKGSNRISLAIQGaHEASVFALCMLRNG-TLVSGGKDRKLISWD-ENFQKIQTVEVPE 517
Cdd:COG2319   126 VAFSPDGKTLaSGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGkLLASGSDDGTVRLWDlATGKLLRTLTGHT 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 518 lyGPVRTVAEGR-GETVLIGTTKNYVLQGSLN-GEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHIYLWDSDSHQPIW 595
Cdd:COG2319   205 --GAVRSVAFSPdGKLLASGSADGTVRLWDLAtGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 596 TKT-LEDSAQSAGFHPSGATVAVGMQTGRWLVLDTESKDLVTVHTDGNEQLSVIRFSPDGNFLAIGSHDNYIYIYAVAEN 674
Cdd:COG2319   283 TLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1207128528 675 GkkysRVGKCSGHSSFITHLDWSVDSQYLVSNSGDYEILYW 715
Cdd:COG2319   363 E----LLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 282-587 3.94e-26

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 109.35  E-value: 3.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 282 RHYTGHTDDIKCLAVHPDKITIATGqvagtSSDGKqlaphVRVWDSVSLNTLHIL-GNGFFDRALVCLSFSKsnggsWLC 360
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLkGHTGPVRDVAASADGT-----YLA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 361 VVddSNDHMLSVWDWQREDRLAEVKCSNESVFAADFHPtDANIIVTCGKSH-LCFWSLEKGSLVkkqglFEKQEKPKFVL 439
Cdd:cd00200    68 SG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGKCL-----TTLRGHTDWVN 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 440 CVTFSENGDAIT-GDSSGNILVWGKGSNRISLAIQGaHEASVFALCMLRNG-TLVSGGKDRKLISWD-ENFQKIQTVEVP 516
Cdd:cd00200   140 SVAFSPDGTFVAsSSQDGTIKLWDLRTGKCVATLTG-HTGEVNSVAFSPDGeKLLSSSSDGTIKLWDlSTGKCLGTLRGH 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207128528 517 ElyGPVRTVAEGRGETVLIGTTKNYVLQG--SLNGEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHIYLWD 587
Cdd:cd00200   219 E--NGVNSVAFSPDGYLLASGSEDGTIRVwdLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 615-699 1.12e-04

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 41.49  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 615 VAVGMQTGRWLVLDTESKDLVTVHTDgNEQLSV--IRFSPDGNFLAIGSHDNYIYIYAvAENGKKysrVGKCSGHSSFIT 692
Cdd:pfam12894  10 IALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLD-AENGKI---VHHFSAGSDLIT 84


                  ....*..
gi 1207128528 693 HLDWSVD 699
Cdd:pfam12894  85 CLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 556-587 6.14e-04

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: 38.06  E-value: 6.14e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1207128528  556 QGHTDELWGLTIHPLKHQFLTCGHDKHIYLWD 587
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 279-326 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 1207128528  279 QLQRHYTGHTDDIKCLAVHPDKITIATGqvagtSSDGKqlaphVRVWD 326
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
279-326 1.78e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 1.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207128528 279 QLQRHYTGHTDDIKCLAVHPDKITIATGqvagtSSDGkqlapHVRVWD 326
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 ...
 205-276 9.61e-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: 140.77  E-value: 9.61e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207128528 205 KMYLKGRPITMYMPKDLVDTYCLETKADLPPKKLKLDWVYGYRGRDCRSNLYLLPTGETVYFIASVVVLYNV 276
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 22-79 4.17e-37

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


Pssm-ID: 409268  Cd Length: 58  Bit Score: 132.92  E-value: 4.17e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207128528  22 NDDSASATSSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNKK 79
Cdd:cd21947     1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
361-715 1.02e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 137.35  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 361 VVDDSNDHMLSVWDWQREDRLAEVKCSNESVFAADFHPTDANIIVTCGKSHLCFWSLEKGSLvkkqgLFEKQEKPKFVLC 440
Cdd:COG2319    51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL-----LRTLTGHTGAVRS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 441 VTFSENGDAI-TGDSSGNILVWGKGSNRISLAIQGaHEASVFALCMLRNG-TLVSGGKDRKLISWD-ENFQKIQTVEVPE 517
Cdd:COG2319   126 VAFSPDGKTLaSGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGkLLASGSDDGTVRLWDlATGKLLRTLTGHT 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 518 lyGPVRTVAEGR-GETVLIGTTKNYVLQGSLN-GEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHIYLWDSDSHQPIW 595
Cdd:COG2319   205 --GAVRSVAFSPdGKLLASGSADGTVRLWDLAtGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 596 TKT-LEDSAQSAGFHPSGATVAVGMQTGRWLVLDTESKDLVTVHTDGNEQLSVIRFSPDGNFLAIGSHDNYIYIYAVAEN 674
Cdd:COG2319   283 TLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1207128528 675 GkkysRVGKCSGHSSFITHLDWSVDSQYLVSNSGDYEILYW 715
Cdd:COG2319   363 E----LLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 COG2319
WD40 repeat [General function prediction only];
361-830 4.45e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 126.56  E-value: 4.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 361 VVDDSNDHMLSVWDWQREDRLAEVKCSNESVFAADFHPTDANIIVTCGKSHLCFWSLEKGSLVKKQglfekQEKPKFVLC 440
Cdd:COG2319     9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATL-----LGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 441 VTFSENGDAI-TGDSSGNILVWGKGSNRISLAIQGaHEASVFALCMLRNG-TLVSGGKDRKLISWDenfqkiqtvevpel 518
Cdd:COG2319    84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSADGTVRLWD-------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 519 ygpVRTvaegrgetvligttknyvlqgslnGEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHIYLWDSDSHQPIWT-K 597
Cdd:COG2319   149 ---LAT------------------------GKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlT 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 598 TLEDSAQSAGFHPSGATVAVGMQTGRWLVLDTESKDLVTVHTDGNEQLSVIRFSPDGNFLAIGSHDNYIYIYAVAENgkk 677
Cdd:COG2319   202 GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG--- 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 678 ySRVGKCSGHSSFITHLDWSVDSQYLVSNSGDYEILYWipsvckqvvSVETTRDIEwatftcTLGFHVfglwpdgsdgTD 757
Cdd:COG2319   279 -ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW---------DLATGKLLR------TLTGHT----------GA 332

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207128528 758 INAVCSSYAKRLLVTGDDFGKVHLFSFpcsQSRAPSHIYSGHSSHVTNVNFLFDDSHLVStGGKDMSIMQWRV 830
Cdd:COG2319   333 VRSVAFSPDGKTLASGSDDGTVRLWDL---ATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
270-672 5.14e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 114.24  E-value: 5.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 270 VVVLYNVDEQLQRHYTGHTDDIKCLAVHPDKITIATGQVAGTssdgkqlaphVRVWDSVSLNTLHILGNgfFDRALVCLS 349
Cdd:COG2319    60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT----------VRLWDLATGLLLRTLTG--HTGAVRSVA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 350 FSKSngGSWLcvVDDSNDHMLSVWDWQREDRLAEVKCSNESVFAADFHPtDANIIVTCGKSH-LCFWSLEKGSLVKkqgl 428
Cdd:COG2319   128 FSPD--GKTL--ASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGtVRLWDLATGKLLR---- 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 429 fEKQEKPKFVLCVTFSENGDAI-TGDSSGNILVWGKGSNRISLAIQGaHEASVFALCMLRNG-TLVSGGKDRKLISWDen 506
Cdd:COG2319   199 -TLTGHTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTG-HSGSVRSVAFSPDGrLLASGSADGTVRLWD-- 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 507 fqkiqtvevpelygpVRTvaegrgetvligttknyvlqgslnGEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHIYLW 586
Cdd:COG2319   275 ---------------LAT------------------------GELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 587 DSDSHQPIWT-KTLEDSAQSAGFHPSGATVAVGMQTGRWLVLDTESKDLVTVHTDGNEQLSVIRFSPDGNFLAIGSHDNY 665
Cdd:COG2319   316 DLATGKLLRTlTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395


                  ....*..
gi 1207128528 666 IYIYAVA 672
Cdd:COG2319   396 VRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 282-587 3.94e-26

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 109.35  E-value: 3.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 282 RHYTGHTDDIKCLAVHPDKITIATGqvagtSSDGKqlaphVRVWDSVSLNTLHIL-GNGFFDRALVCLSFSKsnggsWLC 360
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLkGHTGPVRDVAASADGT-----YLA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 361 VVddSNDHMLSVWDWQREDRLAEVKCSNESVFAADFHPtDANIIVTCGKSH-LCFWSLEKGSLVkkqglFEKQEKPKFVL 439
Cdd:cd00200    68 SG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGKCL-----TTLRGHTDWVN 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 440 CVTFSENGDAIT-GDSSGNILVWGKGSNRISLAIQGaHEASVFALCMLRNG-TLVSGGKDRKLISWD-ENFQKIQTVEVP 516
Cdd:cd00200   140 SVAFSPDGTFVAsSSQDGTIKLWDLRTGKCVATLTG-HTGEVNSVAFSPDGeKLLSSSSDGTIKLWDlSTGKCLGTLRGH 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207128528 517 ElyGPVRTVAEGRGETVLIGTTKNYVLQG--SLNGEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHIYLWD 587
Cdd:cd00200   219 E--NGVNSVAFSPDGYLLASGSEDGTIRVwdLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
271-590 7.82e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.77  E-value: 7.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 271 VVLYNVD-EQLQRHYTGHTDDIKCLAVHPDKITIATGqvagtSSDGKqlaphVRVWDSVSLNTLHILGNGffDRALVCLS 349
Cdd:COG2319   102 VRLWDLAtGLLLRTLTGHTGAVRSVAFSPDGKTLASG-----SADGT-----VRLWDLATGKLLRTLTGH--SGAVTSVA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 350 FSKSngGSWLcvVDDSNDHMLSVWDWQREDRLAEVKCSNESVFAADFHPtDANIIVTCGKSH-LCFWSLEKGSLVKkqgl 428
Cdd:COG2319   170 FSPD--GKLL--ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATGKLLR---- 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 429 fEKQEKPKFVLCVTFSENGDAI-TGDSSGNILVWGKGSNRIsLAIQGAHEASVFALCMLRNG-TLVSGGKDRKLISWD-E 505
Cdd:COG2319   241 -TLTGHSGSVRSVAFSPDGRLLaSGSADGTVRLWDLATGEL-LRTLTGHSGGVNSVAFSPDGkLLASGSDDGTVRLWDlA 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 506 NFQKIQTVEVPElyGPVRTVA-EGRGETVLIGTTKNYV-LQGSLNGEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHI 583
Cdd:COG2319   319 TGKLLRTLTGHT--GAVRSVAfSPDGKTLASGSDDGTVrLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTV 396


                  ....*..
gi 1207128528 584 YLWDSDS 590
Cdd:COG2319   397 RLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 476-829 2.43e-21

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 95.09  E-value: 2.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 476 HEASVFALCMLRNG-TLVSGGKDRKLISWDenfqkiqtvevpelygpvrtVAEGRGETVLigttknyvlqgslngefipi 554
Cdd:cd00200     8 HTGGVTCVAFSPDGkLLATGSGDGTIKVWD--------------------LETGELLRTL-------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 555 tQGHTDELWGLTIHPLKHQFLTCGHDKHIYLWDSDSHQPIWT-KTLEDSAQSAGFHPSGATVAVGMQTGRWLVLDTESKD 633
Cdd:cd00200    48 -KGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTlTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGK 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 634 LVTV---HTDGneqLSVIRFSPDGNFLAIGSHDNYIYIYAVAENgkkySRVGKCSGHSSFITHLDWSVDSQYLVSNSGDY 710
Cdd:cd00200   127 CLTTlrgHTDW---VNSVAFSPDGTFVASSSQDGTIKLWDLRTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDG 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 711 EILYWipsvckqvvsvettrDIEWATFTCTLGFHvfglwpdgsdGTDINAVCSSYAKRLLVTGDDFGKVHLFSfpcSQSR 790
Cdd:cd00200   200 TIKLW---------------DLSTGKCLGTLRGH----------ENGVNSVAFSPDGYLLASGSEDGTIRVWD---LRTG 251

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1207128528 791 APSHIYSGHSSHVTNVNFLFDDSHLVStGGKDMSIMQWR 829
Cdd:cd00200   252 ECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIWD 289
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 20-78 6.50e-20

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


Pssm-ID: 409271  Cd Length: 59  Bit Score: 83.88  E-value: 6.50e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207128528  20 FCNDDSASATSSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNK 78
Cdd:cd21950     1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 32-79 3.70e-19

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: 81.41  E-value: 3.70e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207128528  32 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNKK 79
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 32-74 1.29e-17

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


Pssm-ID: 409267  Cd Length: 44  Bit Score: 76.81  E-value: 1.29e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1207128528  32 MEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQA 74
Cdd:cd21931     1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSS 43
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 277-504 1.19e-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: 81.23  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 277 DEQLQRHYTGHTDDIKCLAVHPDKiTIatgqVAGTSSDGKqlaphVRVWDSVSLNTLHILgnGFFDRALVCLSFSKSNG- 355
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDG-RI----LSSSSRDKT-----IKVWDVETGKCLTTL--RGHTDWVNSVAFSPDGTf 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 356 --GSwlcvvddSNDHMLSVWDwqredrLAEVKC------SNESVFAADFHPTDANIIVTCGKSHLCFWSLEKGSLVKkqg 427
Cdd:cd00200   150 vaSS-------SQDGTIKLWD------LRTGKCvatltgHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLG--- 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207128528 428 LFEKQEkpKFVLCVTFSENGD-AITGDSSGNILVWGKGSNRISLAIQGaHEASVFALCMLRNG-TLVSGGKDRKLISWD 504
Cdd:cd00200   214 TLRGHE--NGVNSVAFSPDGYlLASGSEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGkRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 556-830 3.59e-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: 76.99  E-value: 3.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 556 QGHTDELWGLTIHPLKHQFLTCGHDKHIYLWDSDSHQPIWT-KTLEDSAQSAGFHPSGATVAVGMQTGRWLVLDTESKDL 634
Cdd:cd00200     6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGEC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 635 VTVHTDGNEQLSVIRFSPDGNFLAIGSHDNYIYIYAVAENGKKYSrvgkCSGHSSFITHLDWSVDSQYLVSNSGDYEILY 714
Cdd:cd00200    86 VRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT----LRGHTDWVNSVAFSPDGTFVASSSQDGTIKL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 715 WipsvckqvvsvettrDIEwaTFTCtlgFHVFglwpDGSDGtDINAVCSSYAKRLLVTGDDFGKVHLFSFpcsQSRAPSH 794
Cdd:cd00200   162 W---------------DLR--TGKC---VATL----TGHTG-EVNSVAFSPDGEKLLSSSSDGTIKLWDL---STGKCLG 213

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1207128528 795 IYSGHSSHVTNVNFLfDDSHLVSTGGKDMSIMQWRV 830
Cdd:cd00200   214 TLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDL 248
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 28-72 7.05e-12

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


Pssm-ID: 409270  Cd Length: 48  Bit Score: 60.81  E-value: 7.05e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1207128528  28 ATSSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQ 72
Cdd:cd21949     1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 615-699 1.12e-04

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 41.49  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 615 VAVGMQTGRWLVLDTESKDLVTVHTDgNEQLSV--IRFSPDGNFLAIGSHDNYIYIYAvAENGKKysrVGKCSGHSSFIT 692
Cdd:pfam12894  10 IALATEDGELLLHRLNWQRVWTLSPD-KEDLEVtsLAWRPDGKLLAVGYSDGTVRLLD-AENGKI---VHHFSAGSDLIT 84


                  ....*..
gi 1207128528 693 HLDWSVD 699
Cdd:pfam12894  85 CLGWGEN 91
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 556-587 6.14e-04

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: 38.06  E-value: 6.14e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1207128528  556 QGHTDELWGLTIHPLKHQFLTCGHDKHIYLWD 587
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
574-709 1.08e-03

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 41.60  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207128528 574 FLTCGHDKHIYLWDSDSHQPIWTKTLEDSAQSAGFHPSGATVAV-GMQTGRWLVLDTESKDLVTVHTDGNeQLSVIRFSP 652
Cdd:COG3391    83 YVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVaDSGNGRVSVIDTATGKVVATIPVGA-GPHGIAVDP 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207128528 653 DGNFLAIGSHDN---YIYIYAV-AENGKKYSRVGKcsghSSFITHLDWSVDSQYL-VSNSGD 709
Cdd:COG3391   162 DGKRLYVANSGSntvSVIVSVIdTATGKVVATIPV----GGGPVGVAVSPDGRRLyVANRGS 219
WD40 pfam00400
WD domain, G-beta repeat;
549-587 1.09e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 1.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1207128528 549 GEFIPITQGHTDELWGLTIHPLKHQFLTCGHDKHIYLWD 587
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 279-326 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 1207128528  279 QLQRHYTGHTDDIKCLAVHPDKITIATGqvagtSSDGKqlaphVRVWD 326
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
279-326 1.78e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 1.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207128528 279 QLQRHYTGHTDDIKCLAVHPDKITIATGqvagtSSDGkqlapHVRVWD 326
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 39
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 648-704 2.81e-03

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 41.56  E-value: 2.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207128528  648 IRFSPDGNFLAIGSHDNYIYIYAVAenGKKYSRVGKcSGHSSFITHLDWSVDSQYLV 704
Cdd:COG4946    394 PVWSPDGKKIAFTDNRGRLWVVDLA--SGKVRKVDT-DGYGDGISDLAWSPDSKWLA 447
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 681-715 9.77e-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: 9.77e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1207128528  681 VGKCSGHSSFITHLDWSVDSQYLVSNSGDYEILYW 715
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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