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Conserved domains on  [gi|71834606|ref|NP_001025406|]
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echinoderm microtubule-associated protein-like 2 [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 ...
 178-249 5.61e-38

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: 135.76  E-value: 5.61e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71834606   178 RMFLRGRPITTHIPDQLRDSYSLESKVALPERKLKLQWVYGYRGRDCRSNLYLLPTGEIVYFNASVVVLYNV 249
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
334-802 1.40e-36

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 142.74  E-value: 1.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 334 AVDDANDHILSVWDWQKEKQLAEVKCSNDSVLGAVFHPMEANLIVTCGKSHINFWTVEGSTLTKRqglFEKHEKPkyVLC 413
Cdd:COG2319   9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT---LLGHTAA--VLS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 414 IAFAENGDAI-TGDSSGNIYIWAKGGNRISKVVSGaHEGGIFSLCVLKDG-TLVSGGGkDRKVLLWDhdyrkksemevpe 491
Cdd:COG2319  84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSA-DGTVRLWD------------- 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 492 afgpvrtLAEGKqdelfvgttknavlrgsfsgsLTPIVQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWDTCSHLPLWT- 570
Cdd:COG2319 149 -------LATGK---------------------LLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 571 KAIEDPARSVGFHPSGTVVAVGTMTAKWLVLDTDTRDLV-SMHTDGNEIISVVkYSPDGAYLAVGSHDNFVYIYSVTENg 649
Cdd:COG2319 201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLrTLTGHSGSVRSVA-FSPDGRLLASGSADGTVRLWDLATG- 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 650 kkySRVGKCTGHSSFVTHLDWSTDSQFIVTNSGDYEILYWEASSGKhitnndIVRNLEwatstcvlgfsvfgiwpdgADG 729
Cdd:COG2319 279 ---ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGK------LLRTLT-------------------GHT 330

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71834606 730 TDINAVCRSHDKNLLASADDFGKVHLFSnpcSQPRAPSHIYGGHSSHVTNVAFLHDDSHLIStGGKDTSILQW 802
Cdd:COG2319 331 GAVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 33-80 1.85e-16

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: 73.70  E-value: 1.85e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 71834606  33 MEMDDRLSHLEQRVQLQEDEIQLLKAALADALRRLGCCEEITQASNKK 80
Cdd:cd21948   1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 pfam00400
WD domain, G-beta repeat;
252-299 8.36e-03

WD domain, G-beta repeat;


:

Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 8.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 71834606   252 QQQRHYLGHNDDVKCLAIHPDMVTIATGqvagtSKDGkalppHVRVWD 299
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 ...
 178-249 5.61e-38

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: 135.76  E-value: 5.61e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71834606   178 RMFLRGRPITTHIPDQLRDSYSLESKVALPERKLKLQWVYGYRGRDCRSNLYLLPTGEIVYFNASVVVLYNV 249
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
334-802 1.40e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 142.74  E-value: 1.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 334 AVDDANDHILSVWDWQKEKQLAEVKCSNDSVLGAVFHPMEANLIVTCGKSHINFWTVEGSTLTKRqglFEKHEKPkyVLC 413
Cdd:COG2319   9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT---LLGHTAA--VLS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 414 IAFAENGDAI-TGDSSGNIYIWAKGGNRISKVVSGaHEGGIFSLCVLKDG-TLVSGGGkDRKVLLWDhdyrkksemevpe 491
Cdd:COG2319  84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSA-DGTVRLWD------------- 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 492 afgpvrtLAEGKqdelfvgttknavlrgsfsgsLTPIVQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWDTCSHLPLWT- 570
Cdd:COG2319 149 -------LATGK---------------------LLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 571 KAIEDPARSVGFHPSGTVVAVGTMTAKWLVLDTDTRDLV-SMHTDGNEIISVVkYSPDGAYLAVGSHDNFVYIYSVTENg 649
Cdd:COG2319 201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLrTLTGHSGSVRSVA-FSPDGRLLASGSADGTVRLWDLATG- 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 650 kkySRVGKCTGHSSFVTHLDWSTDSQFIVTNSGDYEILYWEASSGKhitnndIVRNLEwatstcvlgfsvfgiwpdgADG 729
Cdd:COG2319 279 ---ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGK------LLRTLT-------------------GHT 330

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71834606 730 TDINAVCRSHDKNLLASADDFGKVHLFSnpcSQPRAPSHIYGGHSSHVTNVAFLHDDSHLIStGGKDTSILQW 802
Cdd:COG2319 331 GAVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 449-802 3.95e-28

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: 115.12  E-value: 3.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 449 HEGGIFSLCVLKDG-TLVSGGGkDRKVLLWDhdyrkkseMEVPEafgPVRTLaegkqdelfvgttknavlrgsfsgsltp 527
Cdd:cd00200   8 HTGGVTCVAFSPDGkLLATGSG-DGTIKVWD--------LETGE---LLRTL---------------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 528 ivQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWDTCSHLPLWT-KAIEDPARSVGFHPSGTVVAVGTMTAKWLVLDTDTR 606
Cdd:cd00200  48 --KGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTlTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 607 DLVSM---HTDGneiISVVKYSPDGAYLAVGSHDNFVYIYSVTENgkkySRVGKCTGHSSFVTHLDWSTDSQFIVTNSGD 683
Cdd:cd00200 126 KCLTTlrgHTDW---VNSVAFSPDGTFVASSSQDGTIKLWDLRTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSD 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 684 YEILYWEASSGKHItnNDIVRNLEWatstcvlgfsvfgiwpdgadgtdINAVCRSHDKNLLASADDFGKVHLFSnpcSQP 763
Cdd:cd00200 199 GTIKLWDLSTGKCL--GTLRGHENG-----------------------VNSVAFSPDGYLLASGSEDGTIRVWD---LRT 250

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 71834606 764 RAPSHIYGGHSSHVTNVAFlHDDSHLISTGGKDTSILQW 802
Cdd:cd00200 251 GECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIW 288
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 33-80 1.85e-16

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: 73.70  E-value: 1.85e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 71834606  33 MEMDDRLSHLEQRVQLQEDEIQLLKAALADALRRLGCCEEITQASNKK 80
Cdd:cd21948   1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 522-561 9.08e-05

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: 40.37  E-value: 9.08e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 71834606    522 SGSLTPIVQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWD 561
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
523-561 4.03e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 4.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 71834606   523 GSLTPIVQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWD 561
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
252-299 8.36e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 8.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 71834606   252 QQQRHYLGHNDDVKCLAIHPDMVTIATGqvagtSKDGkalppHVRVWD 299
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 ...
 178-249 5.61e-38

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: 135.76  E-value: 5.61e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71834606   178 RMFLRGRPITTHIPDQLRDSYSLESKVALPERKLKLQWVYGYRGRDCRSNLYLLPTGEIVYFNASVVVLYNV 249
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
334-802 1.40e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 142.74  E-value: 1.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 334 AVDDANDHILSVWDWQKEKQLAEVKCSNDSVLGAVFHPMEANLIVTCGKSHINFWTVEGSTLTKRqglFEKHEKPkyVLC 413
Cdd:COG2319   9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT---LLGHTAA--VLS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 414 IAFAENGDAI-TGDSSGNIYIWAKGGNRISKVVSGaHEGGIFSLCVLKDG-TLVSGGGkDRKVLLWDhdyrkksemevpe 491
Cdd:COG2319  84 VAFSPDGRLLaSASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGkTLASGSA-DGTVRLWD------------- 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 492 afgpvrtLAEGKqdelfvgttknavlrgsfsgsLTPIVQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWDTCSHLPLWT- 570
Cdd:COG2319 149 -------LATGK---------------------LLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 571 KAIEDPARSVGFHPSGTVVAVGTMTAKWLVLDTDTRDLV-SMHTDGNEIISVVkYSPDGAYLAVGSHDNFVYIYSVTENg 649
Cdd:COG2319 201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLrTLTGHSGSVRSVA-FSPDGRLLASGSADGTVRLWDLATG- 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 650 kkySRVGKCTGHSSFVTHLDWSTDSQFIVTNSGDYEILYWEASSGKhitnndIVRNLEwatstcvlgfsvfgiwpdgADG 729
Cdd:COG2319 279 ---ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGK------LLRTLT-------------------GHT 330

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71834606 730 TDINAVCRSHDKNLLASADDFGKVHLFSnpcSQPRAPSHIYGGHSSHVTNVAFLHDDSHLIStGGKDTSILQW 802
Cdd:COG2319 331 GAVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
WD40 COG2319
WD40 repeat [General function prediction only];
334-693 7.40e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 140.43  E-value: 7.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 334 AVDDANDHILSVWDWQKEKQLAEVKCSNDSVLGAVFHPMEANLIVTCGKSHINFWTVEGStltKRQGLFEKHEKPkyVLC 413
Cdd:COG2319  51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG---LLLRTLTGHTGA--VRS 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 414 IAFAENGDAI-TGDSSGNIYIWAKGGNRISKVVSGaHEGGIFSLCVLKDGTLVSGGGKDRKVLLWDHDYRKKSEmEVPEA 492
Cdd:COG2319 126 VAFSPDGKTLaSGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR-TLTGH 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 493 FGPVRTLA---EGKQdeLFVGTTKNAVLRGSF-SGSLTPIVQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWDTCSHLPL 568
Cdd:COG2319 204 TGAVRSVAfspDGKL--LASGSADGTVRLWDLaTGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELL 281

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 569 WT-KAIEDPARSVGFHPSGTVVAVGTMTAKWLVLDTDTRDLVSMHTDGNEIISVVKYSPDGAYLAVGSHDNFVYIYSVTE 647
Cdd:COG2319 282 RTlTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 71834606 648 NGkkysRVGKCTGHSSFVTHLDWSTDSQFIVTNSGDYEILYWEASS 693
Cdd:COG2319 362 GE----LLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 449-802 3.95e-28

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: 115.12  E-value: 3.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 449 HEGGIFSLCVLKDG-TLVSGGGkDRKVLLWDhdyrkkseMEVPEafgPVRTLaegkqdelfvgttknavlrgsfsgsltp 527
Cdd:cd00200   8 HTGGVTCVAFSPDGkLLATGSG-DGTIKVWD--------LETGE---LLRTL---------------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 528 ivQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWDTCSHLPLWT-KAIEDPARSVGFHPSGTVVAVGTMTAKWLVLDTDTR 606
Cdd:cd00200  48 --KGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTlTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 607 DLVSM---HTDGneiISVVKYSPDGAYLAVGSHDNFVYIYSVTENgkkySRVGKCTGHSSFVTHLDWSTDSQFIVTNSGD 683
Cdd:cd00200 126 KCLTTlrgHTDW---VNSVAFSPDGTFVASSSQDGTIKLWDLRTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSD 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 684 YEILYWEASSGKHItnNDIVRNLEWatstcvlgfsvfgiwpdgadgtdINAVCRSHDKNLLASADDFGKVHLFSnpcSQP 763
Cdd:cd00200 199 GTIKLWDLSTGKCL--GTLRGHENG-----------------------VNSVAFSPDGYLLASGSEDGTIRVWD---LRT 250

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 71834606 764 RAPSHIYGGHSSHVTNVAFlHDDSHLISTGGKDTSILQW 802
Cdd:cd00200 251 GECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 255-561 7.98e-28

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 113.97  E-value: 7.98e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 255 RHYLGHNDDVKCLAIHPDMVTIATGqvagtSKDGKalpphVRVWDSVSLNTLHVI-GAGVFDRAVTCVAFSKSnggahLC 333
Cdd:cd00200   3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLkGHTGPVRDVAASADGTY-----LA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 334 AVddANDHILSVWDWQKEKQLAEVKCSNDSVLGAVFHPMEaNLIVTCGKSH-INFWTVEGSTLTKRqglFEKHEKPkyVL 412
Cdd:cd00200  68 SG--SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDG-RILSSSSRDKtIKVWDVETGKCLTT---LRGHTDW--VN 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 413 CIAFAENGDAIT-GDSSGNIYIWAKGGNRISKVVSGaHEGGIFSLCVLKDGTLVSGGGKDRKVLLWDHdyRKKSEMEVPE 491
Cdd:cd00200 140 SVAFSPDGTFVAsSSQDGTIKLWDLRTGKCVATLTG-HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL--STGKCLGTLR 216

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71834606 492 AF-GPVRTLAEGKQDELFVGTTKNAVLRG--SFSGSLTPIVQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWD 561
Cdd:cd00200 217 GHeNGVNSVAFSPDGYLLASGSEDGTIRVwdLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 408-695 7.18e-22

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: 96.64  E-value: 7.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 408 PKYVLCIAFAENGDAI-TGDSSGNIYIWAKGGNRISKVVSGaHEGGIFSLCVLKDGTLVSGGGKDRKVLLWDhdyrkkse 486
Cdd:cd00200   9 TGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWD-------- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 487 mevPEAFGPVRTLAegkqdelfvgttknavlrgsfsgsltpivqGHTDELWGLDVHPSTEQFVTCGQDKQVCLWDT---- 562
Cdd:cd00200  80 ---LETGECVRTLT------------------------------GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVetgk 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 563 CSHLplwTKAIEDPARSVGFHPSGTVVAVGT--MTAK-WlvlDTDTRDLVSMHTDGNEIISVVKYSPDGAYLAVGSHDNF 639
Cdd:cd00200 127 CLTT---LRGHTDWVNSVAFSPDGTFVASSSqdGTIKlW---DLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGT 200

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71834606 640 VYIYSVTEnGKKysrVGKCTGHSSFVTHLDWSTDSQFIVTNSGDYEILYWEASSGK 695
Cdd:cd00200 201 IKLWDLST-GKC---LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGE 252
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 246-478 1.36e-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: 92.78  E-value: 1.36e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 246 LYNVEEQQQRHYL-GHNDDVKCLAIHPDMVTIATGQVAGTskdgkalpphVRVWDSVSLNTLHVIGAgvFDRAVTCVAFS 324
Cdd:cd00200  77 LWDLETGECVRTLtGHTSYVSSVAFSPDGRILSSSSRDKT----------IKVWDVETGKCLTTLRG--HTDWVNSVAFS 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 325 KSNG---GAHlcavddaNDHILSVWDWQKEKQLAEVKCSNDSVLGAVFHPMEANLIVTCGKSHINFWTVEGSTLTKrqgL 401
Cdd:cd00200 145 PDGTfvaSSS-------QDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLG---T 214

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71834606 402 FEKHEKPkyVLCIAFAENGD-AITGDSSGNIYIWAKGGNRISKVVSGaHEGGIFSLCVLKDGTLVSGGGKDRKVLLWD 478
Cdd:cd00200 215 LRGHENG--VNSVAFSPDGYlLASGSEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 33-80 1.85e-16

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: 73.70  E-value: 1.85e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 71834606  33 MEMDDRLSHLEQRVQLQEDEIQLLKAALADALRRLGCCEEITQASNKK 80
Cdd:cd21948   1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 23-80 3.04e-13

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: 64.74  E-value: 3.04e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71834606  23 NDDNVSAGGGMEMDDRLSHLEQRVQLQEDEIQLLKAALADALRRLGCCEEITQASNKK 80
Cdd:cd21947   1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
581-805 2.50e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.84  E-value: 2.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 581 GFHPSGTVVAVGTMTAKWLVLDTDTRDLVSMHTDGNEIISVVKYSPDGAYLAVGSHDNFVYIYSVTENGKKYSRvgkcTG 660
Cdd:COG2319   1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATL----LG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 661 HSSFVTHLDWSTDSQFIVTNSGDYEILYWEASSGKHITnndivrnlewatstcvlgfsvfgiwPDGADGTDINAVCRSHD 740
Cdd:COG2319  77 HTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLR-------------------------TLTGHTGAVRSVAFSPD 131

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71834606 741 KNLLASADDFGKVHLFSnpcSQPRAPSHIYGGHSSHVTNVAFlHDDSHLISTGGKDTSILQWVLA 805
Cdd:COG2319 132 GKTLASGSADGTVRLWD---LATGKLLRTLTGHSGAVTSVAF-SPDGKLLASGSDDGTVRLWDLA 192
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 22-79 4.71e-07

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: 47.29  E-value: 4.71e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71834606  22 CNDDNVSAGGGMEMDDRLSHLEQRVQLQEDEIQLLKAALADALRRLGCCEEITQASNK 79
Cdd:cd21950   2 SLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 33-72 2.01e-05

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: 42.14  E-value: 2.01e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 71834606  33 MEMDDRLSHLEQRVQLQEDEIQLLKAALADALRRLGCCEE 72
Cdd:cd21931   1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLET 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 522-561 9.08e-05

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: 40.37  E-value: 9.08e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 71834606    522 SGSLTPIVQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWD 561
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
523-561 4.03e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 4.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 71834606   523 GSLTPIVQGHTDELWGLDVHPSTEQFVTCGQDKQVCLWD 561
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 600-695 7.88e-04

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 40.81  E-value: 7.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 600 VLDTDTRDLVSMhTDGNEIISVVKYSPDGAYLAVGSHDNFVY-IYSVTENGKKYSRVgkcTGHSSFVTHLDWSTDSQFIV 678
Cdd:COG0823  15 VVDLDGGEPRRL-TNSPGIDTSPAWSPDGRRIAFTSDRGGGPqIYVVDADGGEPRRL---TFGGGYNASPSWSPDGKRLA 90

                        90       100
                ....*....|....*....|
gi 71834606 679 TNS---GDYEILYWEASSGK 695
Cdd:COG0823  91 FVSrsdGRFDIYVLDLDGGA 110
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 655-690 3.46e-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: 35.75  E-value: 3.46e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 71834606    655 VGKCTGHSSFVTHLDWSTDSQFIVTNSGDYEILYWE 690
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
548-683 7.07e-03

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 38.91  E-value: 7.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834606 548 FVTCGQDKQVCLWDTCSHLPLWTKAIEDPARSVGFHPSG-TVVAVGTMTAKWLVLDTDTRDLVSMHTDGNEIISVVkYSP 626
Cdd:COG3391  83 YVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGgRLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIA-VDP 161

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71834606 627 DGAYLAVGSHDN-----FVYIYSvTENGKKYSRVGkcTGHSsfVTHLDWSTDSQFI-VTNSGD 683
Cdd:COG3391 162 DGKRLYVANSGSntvsvIVSVID-TATGKVVATIP--VGGG--PVGVAVSPDGRRLyVANRGS 219
WD40 pfam00400
WD domain, G-beta repeat;
252-299 8.36e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 8.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 71834606   252 QQQRHYLGHNDDVKCLAIHPDMVTIATGqvagtSKDGkalppHVRVWD 299
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASG-----SDDG-----TVKVWD 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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