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Conserved domains on  [gi|1622092533|ref|XP_028597730|]
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echinoderm microtubule-associated protein-like 2 isoform X1 [Podarcis muralis]

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 ...
 157-228 1.28e-39

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: 140.38  E-value: 1.28e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622092533 157 KMFLRGRPIPMFVPDAVVATYSLDAKLDLPHKKLKLDWVYGYRGRDCRANLFLLPTGEIVYFVAAVAVLYNV 228
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
313-783 1.43e-36

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 142.36  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 313 AVDDSNDHVLSVWDWQKEQKLADVKCSNESVLAATFHPTEPTLLITCGKSHIHFWTLEAGSLSKRqgiFEKHEKPkyVLC 392
Cdd:COG2319     9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT---LLGHTAA--VLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 393 VAFTENGDT-VTGDSGGNLYIWGKGGNRiCHAVPGAHEGGIFGLCVLRNGTIVTGGGRDRRVVLWgrdyqklqenevpeg 471
Cdd:COG2319    84 VAFSPDGRLlASASADGTVRLWDLATGL-LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLW--------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 472 fgpvrtiaegkgdslfvgttrnsvlhgSLATGFSLLV-QGHTEELWGLATHPALDQFLTCGQDKQVHLWSVATHQPLWS- 549
Cdd:COG2319   148 ---------------------------DLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 550 KGIEDAARSAGFHPSGSVLVVGTVTGRWLVLDTETRDLVTIHTDGGEPISVVSFSPDGKYLALGSHDNFVYIYLVSEGGR 629
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 630 kygrVGKCSGHSSFITHLDWAFDSSCLVTNSGDYEILYWDPSTCRQITSAEAvrnmdwatatcvlgfgvfgiwpegaDGT 709
Cdd:COG2319   281 ----LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG-------------------------HTG 331

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622092533 710 DINAVCRSHDGKLLASADDFGKVHLFSypcCQPRAPSHTYNGHSSHVTNIAFLHDDSLLLStGGTDTSILQWRL 783
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 12-59 1.84e-25

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: 99.13  E-value: 1.84e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622092533  12 MEVDDRISYLEQRLQLQEDEIQVLKAALADVLRRLSTCEENGLSLQKK 59
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 238-278 8.78e-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: 8.78e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1622092533  238 GHNDDIKCLAVHPDMVTIATGqvagtSKDGKplpphVRVWD 278
Cdd:smart00320  10 GHTGPVTSVAFSPDGKYLASG-----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 ...
 157-228 1.28e-39

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: 140.38  E-value: 1.28e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622092533 157 KMFLRGRPIPMFVPDAVVATYSLDAKLDLPHKKLKLDWVYGYRGRDCRANLFLLPTGEIVYFVAAVAVLYNV 228
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
313-783 1.43e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 142.36  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 313 AVDDSNDHVLSVWDWQKEQKLADVKCSNESVLAATFHPTEPTLLITCGKSHIHFWTLEAGSLSKRqgiFEKHEKPkyVLC 392
Cdd:COG2319     9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT---LLGHTAA--VLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 393 VAFTENGDT-VTGDSGGNLYIWGKGGNRiCHAVPGAHEGGIFGLCVLRNGTIVTGGGRDRRVVLWgrdyqklqenevpeg 471
Cdd:COG2319    84 VAFSPDGRLlASASADGTVRLWDLATGL-LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLW--------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 472 fgpvrtiaegkgdslfvgttrnsvlhgSLATGFSLLV-QGHTEELWGLATHPALDQFLTCGQDKQVHLWSVATHQPLWS- 549
Cdd:COG2319   148 ---------------------------DLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 550 KGIEDAARSAGFHPSGSVLVVGTVTGRWLVLDTETRDLVTIHTDGGEPISVVSFSPDGKYLALGSHDNFVYIYLVSEGGR 629
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 630 kygrVGKCSGHSSFITHLDWAFDSSCLVTNSGDYEILYWDPSTCRQITSAEAvrnmdwatatcvlgfgvfgiwpegaDGT 709
Cdd:COG2319   281 ----LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG-------------------------HTG 331

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622092533 710 DINAVCRSHDGKLLASADDFGKVHLFSypcCQPRAPSHTYNGHSSHVTNIAFLHDDSLLLStGGTDTSILQWRL 783
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 473-782 1.69e-27

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 113.20  E-value: 1.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 473 GPVRTIA-EGKGDSLFVGTTRNSVLHGSLATGFSLLV-QGHTEELWGLATHPALDQFLTCGQDKQVHLWSVATHQPLWS- 549
Cdd:cd00200    10 GGVTCVAfSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTl 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 550 KGIEDAARSAGFHPSGSVLVVGTVTGRWLVLDTETRDLVTI---HTDggePISVVSFSPDGKYLALGSHDNFVYIYLVSE 626
Cdd:cd00200    90 TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTlrgHTD---WVNSVAFSPDGTFVASSSQDGTIKLWDLRT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 627 GGRkygrVGKCSGHSSFITHLDWAFDSSCLVTNSGDYEILYWDPSTCRQITSAEAVRNmdwatatcvlgfgvfgiwpega 706
Cdd:cd00200   167 GKC----VATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHEN---------------------- 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622092533 707 dgtDINAVCRSHDGKLLASADDFGKVHLFSYpccQPRAPSHTYNGHSSHVTNIAFlHDDSLLLSTGGTDTSILQWR 782
Cdd:cd00200   221 ---GVNSVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 12-59 1.84e-25

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: 99.13  E-value: 1.84e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622092533  12 MEVDDRISYLEQRLQLQEDEIQVLKAALADVLRRLSTCEENGLSLQKK 59
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 200-367 4.86e-09

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 58.12  E-value: 4.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 200 GRDCRANLFLLPTGEIVY-------FVAAVAV-----------------LYNVEEQRQRH-YLGHNDDIKCLAVHPDMVT 254
Cdd:cd00200   112 SRDKTIKVWDVETGKCLTtlrghtdWVNSVAFspdgtfvasssqdgtikLWDLRTGKCVAtLTGHTGEVNSVAFSPDGEK 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 255 IATGqvagtSKDGkplppHVRVWDSVSLNTLHVLGPgpFDRAVSCVGFSKSngGGLLCAVDDsnDHVLSVWDWQKEQKLA 334
Cdd:cd00200   192 LLSS-----SSDG-----TIKLWDLSTGKCLGTLRG--HENGVNSVAFSPD--GYLLASGSE--DGTIRVWDLRTGECVQ 255

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622092533 335 DVKCSNESVLAATFHPTEPTlLITCGKSH-IHFW 367
Cdd:cd00200   256 TLSGHTNSVTSLAWSPDGKR-LASGSADGtIRIW 288
PTZ00421 PTZ00421
coronin; Provisional
 598-681 1.63e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 41.80  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 598 ISVVSFSPDGK-YLALGSHDNFVYIYLVSEGgrKYGRVGKCsgHSSFITHLDWAFDSSCLVTNSGDYEILYWDPSTCRQI 676
Cdd:PTZ00421  128 VGIVSFHPSAMnVLASAGADMVVNVWDVERG--KAVEVIKC--HSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIV 203


                  ....*
gi 1622092533 677 TSAEA 681
Cdd:PTZ00421  204 SSVEA 208
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 584-622 5.63e-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: 35.37  E-value: 5.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622092533  584 TRDLVTIHTDGGEPISVVSFSPDGKYLALGSHDNFVYIY 622
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 238-278 8.78e-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: 8.78e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1622092533  238 GHNDDIKCLAVHPDMVTIATGqvagtSKDGKplpphVRVWD 278
Cdd:smart00320  10 GHTGPVTSVAFSPDGKYLASG-----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 ...
 157-228 1.28e-39

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: 140.38  E-value: 1.28e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622092533 157 KMFLRGRPIPMFVPDAVVATYSLDAKLDLPHKKLKLDWVYGYRGRDCRANLFLLPTGEIVYFVAAVAVLYNV 228
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
313-783 1.43e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 142.36  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 313 AVDDSNDHVLSVWDWQKEQKLADVKCSNESVLAATFHPTEPTLLITCGKSHIHFWTLEAGSLSKRqgiFEKHEKPkyVLC 392
Cdd:COG2319     9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT---LLGHTAA--VLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 393 VAFTENGDT-VTGDSGGNLYIWGKGGNRiCHAVPGAHEGGIFGLCVLRNGTIVTGGGRDRRVVLWgrdyqklqenevpeg 471
Cdd:COG2319    84 VAFSPDGRLlASASADGTVRLWDLATGL-LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLW--------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 472 fgpvrtiaegkgdslfvgttrnsvlhgSLATGFSLLV-QGHTEELWGLATHPALDQFLTCGQDKQVHLWSVATHQPLWS- 549
Cdd:COG2319   148 ---------------------------DLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 550 KGIEDAARSAGFHPSGSVLVVGTVTGRWLVLDTETRDLVTIHTDGGEPISVVSFSPDGKYLALGSHDNFVYIYLVSEGGR 629
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 630 kygrVGKCSGHSSFITHLDWAFDSSCLVTNSGDYEILYWDPSTCRQITSAEAvrnmdwatatcvlgfgvfgiwpegaDGT 709
Cdd:COG2319   281 ----LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG-------------------------HTG 331

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622092533 710 DINAVCRSHDGKLLASADDFGKVHLFSypcCQPRAPSHTYNGHSSHVTNIAFLHDDSLLLStGGTDTSILQWRL 783
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
313-672 3.81e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 141.20  E-value: 3.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 313 AVDDSNDHVLSVWDWQKEQKLADVKCSNESVLAATFHPTEPTLLITCGKSHIHFWTLEAGslsKRQGIFEKHEKPkyVLC 392
Cdd:COG2319    51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG---LLLRTLTGHTGA--VRS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 393 VAFTENGDT-VTGDSGGNLYIWGKGGNRICHAVPGaHEGGIFGLCVLRNGTIVTGGGRDRRVVLWGRDYQKLQEnEVPEG 471
Cdd:COG2319   126 VAFSPDGKTlASGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR-TLTGH 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 472 FGPVRTIA---EGKgdSLFVGTTRNSVLHGSLATGFSLLV-QGHTEELWGLATHPALDQFLTCGQDKQVHLWSVATHQPL 547
Cdd:COG2319   204 TGAVRSVAfspDGK--LLASGSADGTVRLWDLATGKLLRTlTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELL 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 548 WS-KGIEDAARSAGFHPSGSVLVVGTVTGRWLVLDTETRDLVTIHTDGGEPISVVSFSPDGKYLALGSHDNFVYIYLVSE 626
Cdd:COG2319   282 RTlTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1622092533 627 GgrkyGRVGKCSGHSSFITHLDWAFDSSCLVTNSGDYEILYWDPST 672
Cdd:COG2319   362 G----ELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
221-622 7.36e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 131.57  E-value: 7.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 221 AVAVLYNVEEQRQRHYLGHNDDIKCLAVHPDMVTIATGQVAGTskdgkplpphVRVWDSVSLNTLHVLgpGPFDRAVSCV 300
Cdd:COG2319    59 TLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT----------VRLWDLATGLLLRTL--TGHTGAVRSV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 301 GFSkSNGGGLLCAvddSNDHVLSVWDWQKEQKLADVKCSNESVLAATFHPTEPTLLITCGKSHIHFWTLEAGslsKRQGI 380
Cdd:COG2319   127 AFS-PDGKTLASG---SADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATG---KLLRT 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 381 FEKHEKPkyVLCVAFTENGDT-VTGDSGGNLYIWGKGGNRiCHAVPGAHEGGIFGLCVLRNGTIVTGGGRDRRVVLWgrd 459
Cdd:COG2319   200 LTGHTGA--VRSVAFSPDGKLlASGSADGTVRLWDLATGK-LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW--- 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 460 yqklqenevpegfgpvrtiaegkgdslfvgttrnsvlhgSLATGFSL-LVQGHTEELWGLATHPALDQFLTCGQDKQVHL 538
Cdd:COG2319   274 ---------------------------------------DLATGELLrTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 539 WSVATHQPLWS-KGIEDAARSAGFHPSGSVLVVGTVTGRWLVLDTETRDLVTIHTDGGEPISVVSFSPDGKYLALGSHDN 617
Cdd:COG2319   315 WDLATGKLLRTlTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADG 394


                  ....*
gi 1622092533 618 FVYIY 622
Cdd:COG2319   395 TVRLW 399
WD40 COG2319
WD40 repeat [General function prediction only];
442-783 8.30e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.49  E-value: 8.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 442 TIVTGGGRDRRVVLWGRDYQKLQENEVPEGFGPVRTIAEGKGDSLFVGTTRNSVLHGSLATGFSLLVQGHTEELWGLATH 521
Cdd:COG2319     8 ALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 522 PALDQFLTCGQDKQVHLWSVATHQPLWS-KGIEDAARSAGFHPSGSVLVVGTVTGRWLVLDTETRDLVTIHTDGGEPISV 600
Cdd:COG2319    88 PDGRLLASASADGTVRLWDLATGLLLRTlTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 601 VSFSPDGKYLALGSHDNFVYIYLVSEGgrkyGRVGKCSGHSSFITHLDWAFDSSCLVTNSGDYEILYWDPSTCRQITsae 680
Cdd:COG2319   168 VAFSPDGKLLASGSDDGTVRLWDLATG----KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR--- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 681 avrnmdwatatcvlgfgvfgiwPEGADGTDINAVCRSHDGKLLASADDFGKVHLFSYpccQPRAPSHTYNGHSSHVTNIA 760
Cdd:COG2319   241 ----------------------TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL---ATGELLRTLTGHSGGVNSVA 295

                         330       340
                  ....*....|....*....|...
gi 1622092533 761 FLHDDSLLLStGGTDTSILQWRL 783
Cdd:COG2319   296 FSPDGKLLAS-GSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 473-782 1.69e-27

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 113.20  E-value: 1.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 473 GPVRTIA-EGKGDSLFVGTTRNSVLHGSLATGFSLLV-QGHTEELWGLATHPALDQFLTCGQDKQVHLWSVATHQPLWS- 549
Cdd:cd00200    10 GGVTCVAfSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTl 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 550 KGIEDAARSAGFHPSGSVLVVGTVTGRWLVLDTETRDLVTI---HTDggePISVVSFSPDGKYLALGSHDNFVYIYLVSE 626
Cdd:cd00200    90 TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTlrgHTD---WVNSVAFSPDGTFVASSSQDGTIKLWDLRT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 627 GGRkygrVGKCSGHSSFITHLDWAFDSSCLVTNSGDYEILYWDPSTCRQITSAEAVRNmdwatatcvlgfgvfgiwpega 706
Cdd:cd00200   167 GKC----VATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHEN---------------------- 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622092533 707 dgtDINAVCRSHDGKLLASADDFGKVHLFSYpccQPRAPSHTYNGHSSHVTNIAFlHDDSLLLSTGGTDTSILQWR 782
Cdd:cd00200   221 ---GVNSVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 234-540 3.70e-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: 3.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 234 RHYLGHNDDIKCLAVHPDMVTIATGqvagtSKDGKplpphVRVWDSVSLNTLHVL-GPGPFDRAVSCVGFSKSngggLLC 312
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLkGHTGPVRDVAASADGTY----LAS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 313 AvddSNDHVLSVWDWQKEQKLADVKCSNESVLAATFHPTePTLLITCGKSH-IHFWTLEAGSLSKrqgIFEKHEKPkyVL 391
Cdd:cd00200    69 G---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD-GRILSSSSRDKtIKVWDVETGKCLT---TLRGHTDW--VN 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 392 CVAFTENGDTVTGDSG-GNLYIWGKGGNRICHAVPGaHEGGIFGLCVLRNGTIVTGGGRDRRVVLWgrDYQKLQENEVPE 470
Cdd:cd00200   140 SVAFSPDGTFVASSSQdGTIKLWDLRTGKCVATLTG-HTGEVNSVAFSPDGEKLLSSSSDGTIKLW--DLSTGKCLGTLR 216

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622092533 471 GF-GPVRTIAEGKGDSLFVGTTRNSVLHG-SLATGFSLLV-QGHTEELWGLATHPALDQFLTCGQDKQVHLWS 540
Cdd:cd00200   217 GHeNGVNSVAFSPDGYLLASGSEDGTIRVwDLRTGECVQTlSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 12-59 1.84e-25

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: 99.13  E-value: 1.84e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622092533  12 MEVDDRISYLEQRLQLQEDEIQVLKAALADVLRRLSTCEENGLSLQKK 59
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 336-669 5.90e-23

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: 99.72  E-value: 5.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 336 VKCSNESVLAATFHPTEPTLLITCGKSHIHFWTLEAGSLSKRqgiFEKHEKPkyVLCVAFTENGDT-VTGDSGGNLYIWG 414
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT---LKGHTGP--VRDVAASADGTYlASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 415 KGGNRICHAVPGaHEGGIFGLCVLRNGTIVTGGGRDRRVVLWgrdyqklqenEVPEGfGPVRTIaegkgdslfvgttrns 494
Cdd:cd00200    80 LETGECVRTLTG-HTSYVSSVAFSPDGRILSSSSRDKTIKVW----------DVETG-KCLTTL---------------- 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 495 vlhgslatgfsllvQGHTEELWGLATHPAlDQFLTCG-QDKQVHLWSVATHQPLWS-KGIEDAARSAGFHPSGSVLVVGT 572
Cdd:cd00200   132 --------------RGHTDWVNSVAFSPD-GTFVASSsQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSS 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 573 VTGRWLVLDTETRDLVTIHTDGGEPISVVSFSPDGKYLALGSHDNFVYIYLVseggRKYGRVGKCSGHSSFITHLDWAFD 652
Cdd:cd00200   197 SDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL----RTGECVQTLSGHTNSVTSLAWSPD 272

                         330
                  ....*....|....*..
gi 1622092533 653 SSCLVTNSGDYEILYWD 669
Cdd:cd00200   273 GKRLASGSADGTIRIWD 289
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 3-59 8.63e-20

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: 83.62  E-value: 8.63e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622092533   3 DDNLSGISGMEVDDRISYLEQRLQLQEDEIQVLKAALADVLRRLSTCEENGLSLQKK 59
Cdd:cd21947     2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNRK 58
WD40 COG2319
WD40 repeat [General function prediction only];
519-783 1.84e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 88.43  E-value: 1.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 519 ATHPALDQFLTCGQDKQVHLWSVATHQPLWS-KGIEDAARSAGFHPSGSVLVVGTVTGRWLVLDTETRDLVTIHTDGGEP 597
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLlLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 598 ISVVSFSPDGKYLALGSHDNFVYIYLVSEGgrkyGRVGKCSGHSSFITHLDWAFDSSCLVTNSGDYEILYWDPSTCRQIT 677
Cdd:COG2319    81 VLSVAFSPDGRLLASASADGTVRLWDLATG----LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 678 SAEAVRNmdwatatcvlgfgvfgiwpegadgtDINAVCRSHDGKLLASADDFGKVHLFSypcCQPRAPSHTYNGHSSHVT 757
Cdd:COG2319   157 TLTGHSG-------------------------AVTSVAFSPDGKLLASGSDDGTVRLWD---LATGKLLRTLTGHTGAVR 208

                         250       260
                  ....*....|....*....|....*.
gi 1622092533 758 NIAFLHDDSLLLStGGTDTSILQWRL 783
Cdd:COG2319   209 SVAFSPDGKLLAS-GSADGTVRLWDL 233
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 550-783 1.94e-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: 80.46  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 550 KGIEDAARSAGFHPSGSVLVVGTVTGRWLVLDTETRDLV---TIHTDggePISVVSFSPDGKYLALGSHDNFVYIYLVSE 626
Cdd:cd00200     6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLrtlKGHTG---PVRDVAASADGTYLASGSSDKTIRLWDLET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 627 GgrkyGRVGKCSGHSSFITHLDWAFDSSCLVTNSGDYEILYWDPSTCRQITSAEAVRnmDWATATCVLGFG--VFGIWpe 704
Cdd:cd00200    83 G----ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHT--DWVNSVAFSPDGtfVASSS-- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 705 gADGT--------------------DINAVCRSHDGKLLASADDFGKVHLFSypcCQPRAPSHTYNGHSSHVTNIAFlHD 764
Cdd:cd00200   155 -QDGTiklwdlrtgkcvatltghtgEVNSVAFSPDGEKLLSSSSDGTIKLWD---LSTGKCLGTLRGHENGVNSVAF-SP 229

                         250
                  ....*....|....*....
gi 1622092533 765 DSLLLSTGGTDTSILQWRL 783
Cdd:cd00200   230 DGYLLASGSEDGTIRVWDL 248
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 2-58 1.94e-15

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: 71.17  E-value: 1.94e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622092533   2 TDDNLSGISGMEVDDRISYLEQRLQLQEDEIQVLKAALADVLRRLSTCEENGLSLQK 58
Cdd:cd21950     3 LDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 12-53 8.37e-15

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: 68.72  E-value: 8.37e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622092533  12 MEVDDRISYLEQRLQLQEDEIQVLKAALADVLRRLSTCEENG 53
Cdd:cd21931     1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRS 42
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 13-51 7.36e-11

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


Pssm-ID: 409270  Cd Length: 48  Bit Score: 57.72  E-value: 7.36e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622092533  13 EVDDRISYLEQRLQLQEDEIQVLKAALADVLRRLSTCEE 51
Cdd:cd21949     6 EAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQ 44
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 200-367 4.86e-09

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 58.12  E-value: 4.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 200 GRDCRANLFLLPTGEIVY-------FVAAVAV-----------------LYNVEEQRQRH-YLGHNDDIKCLAVHPDMVT 254
Cdd:cd00200   112 SRDKTIKVWDVETGKCLTtlrghtdWVNSVAFspdgtfvasssqdgtikLWDLRTGKCVAtLTGHTGEVNSVAFSPDGEK 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 255 IATGqvagtSKDGkplppHVRVWDSVSLNTLHVLGPgpFDRAVSCVGFSKSngGGLLCAVDDsnDHVLSVWDWQKEQKLA 334
Cdd:cd00200   192 LLSS-----SSDG-----TIKLWDLSTGKCLGTLRG--HENGVNSVAFSPD--GYLLASGSE--DGTIRVWDLRTGECVQ 255

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622092533 335 DVKCSNESVLAATFHPTEPTlLITCGKSH-IHFW 367
Cdd:cd00200   256 TLSGHTNSVTSLAWSPDGKR-LASGSADGtIRIW 288
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
527-624 8.03e-05

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


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 45.07  E-value: 8.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 527 FLTCGQDKQVHLWSVATHQPLWSKGIEDAARSAGFHPSGS-VLVVGTVTGRWLVLDTETRDLVTIHTDGGEPISVVsFSP 605
Cdd:COG3391    83 YVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGrLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIA-VDP 161

                          90       100
                  ....*....|....*....|
gi 1622092533 606 DGKYLALGSH-DNFVYIYLV 624
Cdd:COG3391   162 DGKRLYVANSgSNTVSVIVS 181
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 579-672 1.29e-03

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: 40.04  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 579 VLDTETRDLVTIHTDGGEPISVvSFSPDGKYLALGSHDNFVY-IYLVSEGGRKYGRVGKCSGHSSFithLDWAFDSSCLV 657
Cdd:COG0823    15 VVDLDGGEPRRLTNSPGIDTSP-AWSPDGRRIAFTSDRGGGPqIYVVDADGGEPRRLTFGGGYNAS---PSWSPDGKRLA 90

                          90
                  ....*....|....*...
gi 1622092533 658 TNS---GDYEILYWDPST 672
Cdd:COG0823    91 FVSrsdGRFDIYVLDLDG 108
PTZ00421 PTZ00421
coronin; Provisional
 598-681 1.63e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 41.80  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622092533 598 ISVVSFSPDGK-YLALGSHDNFVYIYLVSEGgrKYGRVGKCsgHSSFITHLDWAFDSSCLVTNSGDYEILYWDPSTCRQI 676
Cdd:PTZ00421  128 VGIVSFHPSAMnVLASAGADMVVNVWDVERG--KAVEVIKC--HSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIV 203


                  ....*
gi 1622092533 677 TSAEA 681
Cdd:PTZ00421  204 SSVEA 208
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 584-622 5.63e-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: 35.37  E-value: 5.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622092533  584 TRDLVTIHTDGGEPISVVSFSPDGKYLALGSHDNFVYIY 622
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 745-781 7.14e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.98  E-value: 7.14e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1622092533  745 PSHTYNGHSSHVTNIAFLHDDSLLLStGGTDTSILQW 781
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLAS-GSDDGTIKLW 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 238-278 8.78e-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: 8.78e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1622092533  238 GHNDDIKCLAVHPDMVTIATGqvagtSKDGKplpphVRVWD 278
Cdd:smart00320  10 GHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 509-540 9.88e-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: 9.88e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622092533  509 QGHTEELWGLATHPALDQFLTCGQDKQVHLWS 540
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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