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Conserved domains on  [gi|2462571909|ref|XP_054197381|]
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echinoderm microtubule-associated protein-like 4 isoform X3 [Homo sapiens]

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 ...
 239-307 4.78e-35

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: 127.28  E-value: 4.78e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462571909 239 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 307
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 6-64 2.72e-31

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: 116.24  E-value: 2.72e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462571909   6 GSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21950     1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 COG2319
WD40 repeat [General function prediction only];
397-756 1.26e-23

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.22  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 397 SNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW-SGNSLTRKQGifgkyeKPKFVQCLA 474
Cdd:COG2319    97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLaTGKLLRTLTG------HSGAVTSVA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 475 FLGNGDVL-TGDSGGVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnp 553
Cdd:COG2319   170 FSPDGKLLaSGSDDGTVRLWDLATGKLL------------RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD----- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 554 ereievpdqygtiraVAEGKADQFLvgtsrnfilrgtfndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNsm 633
Cdd:COG2319   233 ---------------LATGKLLRTL---------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWD-- 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 634 ehrLEWTRLVDEPGHCAD------FHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHD 707
Cdd:COG2319   275 ---LATGELLRTLTGHSGgvnsvaFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDD 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462571909 708 NFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEI 756
Cdd:COG2319   352 GTVRLW----DLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTV 396
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 318-358 9.05e-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: 9.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2462571909  318 GHTDCVKCLAIHPDKIRIATGqiagvDKDGrplqpHVRVWD 358
Cdd:smart00320  10 GHTGPVTSVAFSPDGKYLASG-----SDDG-----TIKLWD 40
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 239-307 4.78e-35

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: 127.28  E-value: 4.78e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462571909 239 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 307
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 6-64 2.72e-31

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: 116.24  E-value: 2.72e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462571909   6 GSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21950     1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 COG2319
WD40 repeat [General function prediction only];
397-756 1.26e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.22  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 397 SNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW-SGNSLTRKQGifgkyeKPKFVQCLA 474
Cdd:COG2319    97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLaTGKLLRTLTG------HSGAVTSVA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 475 FLGNGDVL-TGDSGGVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnp 553
Cdd:COG2319   170 FSPDGKLLaSGSDDGTVRLWDLATGKLL------------RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD----- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 554 ereievpdqygtiraVAEGKADQFLvgtsrnfilrgtfndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNsm 633
Cdd:COG2319   233 ---------------LATGKLLRTL---------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWD-- 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 634 ehrLEWTRLVDEPGHCAD------FHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHD 707
Cdd:COG2319   275 ---LATGELLRTLTGHSGgvnsvaFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDD 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462571909 708 NFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEI 756
Cdd:COG2319   352 GTVRLW----DLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTV 396
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 467-753 2.23e-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: 98.18  E-value: 2.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 467 PKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTTVEPtpgkgpkgvyqiSKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKII 545
Cdd:cd00200     9 TGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGEL------------LRTLKGHTGPVRDVAASADGTYLASGSSDKTIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 546 LWD-HDLNPEREIEVPDQYgtIRAVAEGKADQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCA 622
Cdd:cd00200    77 LWDlETGECVRTLTGHTSY--VSSVAFSPDGRILSSSSRDKTIKvwDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 623 QDRQVCLWNSMEHRLEWTRlvdePGH-----CADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSID 697
Cdd:cd00200   155 QDGTIKLWDLRTGKCVATL----TGHtgevnSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462571909 698 GTFLAVGSHDNFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGD 753
Cdd:cd00200   231 GYLLASGSEDGTIRVW----DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSAD 282
WD40 pfam00400
WD domain, G-beta repeat;
600-631 1.40e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.40e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462571909 600 QGHTDELWGLATHPFKDLLLTCAQDRQVCLWN 631
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 600-631 1.65e-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: 36.91  E-value: 1.65e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462571909  600 QGHTDELWGLATHPFKDLLLTCAQDRQVCLWN 631
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 318-358 9.05e-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: 9.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2462571909  318 GHTDCVKCLAIHPDKIRIATGqiagvDKDGrplqpHVRVWD 358
Cdd:smart00320  10 GHTGPVTSVAFSPDGKYLASG-----SDDG-----TIKLWD 40
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 239-307 4.78e-35

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: 127.28  E-value: 4.78e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462571909 239 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 307
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 6-64 2.72e-31

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: 116.24  E-value: 2.72e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462571909   6 GSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21950     1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 COG2319
WD40 repeat [General function prediction only];
397-756 1.26e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.22  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 397 SNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW-SGNSLTRKQGifgkyeKPKFVQCLA 474
Cdd:COG2319    97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLaTGKLLRTLTG------HSGAVTSVA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 475 FLGNGDVL-TGDSGGVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnp 553
Cdd:COG2319   170 FSPDGKLLaSGSDDGTVRLWDLATGKLL------------RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD----- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 554 ereievpdqygtiraVAEGKADQFLvgtsrnfilrgtfndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNsm 633
Cdd:COG2319   233 ---------------LATGKLLRTL---------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWD-- 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 634 ehrLEWTRLVDEPGHCAD------FHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHD 707
Cdd:COG2319   275 ---LATGELLRTLTGHSGgvnsvaFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDD 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462571909 708 NFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEI 756
Cdd:COG2319   352 GTVRLW----DLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTV 396
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 467-753 2.23e-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: 98.18  E-value: 2.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 467 PKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTTVEPtpgkgpkgvyqiSKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKII 545
Cdd:cd00200     9 TGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGEL------------LRTLKGHTGPVRDVAASADGTYLASGSSDKTIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 546 LWD-HDLNPEREIEVPDQYgtIRAVAEGKADQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCA 622
Cdd:cd00200    77 LWDlETGECVRTLTGHTSY--VSSVAFSPDGRILSSSSRDKTIKvwDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 623 QDRQVCLWNSMEHRLEWTRlvdePGH-----CADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSID 697
Cdd:cd00200   155 QDGTIKLWDLRTGKCVATL----TGHtgevnSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462571909 698 GTFLAVGSHDNFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGD 753
Cdd:cd00200   231 GYLLASGSEDGTIRVW----DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSAD 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 314-667 3.44e-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: 91.63  E-value: 3.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 314 RHYLGHTDCVKCLAIHPDKIRIATGqiagvDKDGRplqphVRVWDSVTLStlQIIGLGTFERGVGCLDFSkADSGVHLCV 393
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGE--LLRTLKGHTGPVRDVAAS-ADGTYLASG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 394 iddSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 470
Cdd:cd00200    70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 471 QCLAFLGNGDVLTGDSG-GVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 549
Cdd:cd00200   139 NSVAFSPDGTFVASSSQdGTIKLWDLRTGKCV------------ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 550 dlnpereievpdqygtiravaegkadqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCL 629
Cdd:cd00200   207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2462571909 630 WNsMEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 667
Cdd:cd00200   246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 513-756 4.35e-19

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 88.16  E-value: 4.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 513 SKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnpereievpdqygtiravaegkadqflvgtsrnfilrgTFN 592
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LET 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 593 DGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTrLVdepGH-----CADFHPSGTVVAIGTHSGR 667
Cdd:cd00200    41 GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT-LT---GHtsyvsSVAFSPDGRILSSSSRDKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 668 WFVLDAETRDLVSI---HTDgneqlSVM--RYSIDGTFLAVGSHDNFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSP 742
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLW----DLRTGKCVATLTGHTGEVNSVAFSP 187

                         250
                  ....*....|....
gi 2462571909 743 DNKYIMSNSGDYEI 756
Cdd:cd00200   188 DGEKLLSSSSDGTI 201
WD40 COG2319
WD40 repeat [General function prediction only];
302-713 5.97e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 89.97  E-value: 5.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 302 VVVLFNYEERTQRHYLGHTDCVKCLAIHPDKIRIATGQIAGVdkdgrplqphVRVWDsvTLSTLQIIGLGTFERGVGCLD 381
Cdd:COG2319    60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGT----------VRLWD--LATGLLLRTLTGHTGAVRSVA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 382 FSkAD-----SGvhlcviddSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW-SGNSL 454
Cdd:COG2319   128 FS-PDgktlaSG--------SADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGtVRLWDLaTGKLL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 455 TRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDGSVFTLCQMRNGM 533
Cdd:COG2319   198 RTLTG------HTGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLL------------RTLTGHSGSVRSVAFSPDGR 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 534 LLTGGGKDRKIILWDhdlnpereievpdqygtiraVAEGKADQFLvgtsrnfilrgtfndgfqievQGHTDELWGLATHP 613
Cdd:COG2319   260 LLASGSADGTVRLWD--------------------LATGELLRTL---------------------TGHSGGVNSVAFSP 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 614 FKDLLLTCAQDRQVCLWNSMEHRLEWTRlvdePGH-----CADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQ 688
Cdd:COG2319   299 DGKLLASGSDDGTVRLWDLATGKLLRTL----TGHtgavrSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGA 374

                         410       420
                  ....*....|....*....|....*
gi 2462571909 689 LSVMRYSIDGTFLAVGSHDNFIYLY 713
Cdd:COG2319   375 VTSVAFSPDGRTLASGSADGTVRLW 399
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 9-64 1.36e-18

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: 80.15  E-value: 1.36e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462571909   9 DDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21947     2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNR 57
WD40 COG2319
WD40 repeat [General function prediction only];
311-631 3.26e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 87.66  E-value: 3.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 311 RTQRHYLGHTDCVKCLAIHPDKIRIATGqiagvDKDGRplqphVRVWDSVTLSTLQIigLGTFERGVGCLDFSkAD---- 386
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASG-----SADGT-----VRLWDLATGKLLRT--LTGHSGAVTSVAFS-PDgkll 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 387 -SGvhlcviddSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTWSGNSLTRKQGIFGKY 464
Cdd:COG2319   178 aSG--------SDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATGKLLRTLTGHSGS 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 465 ekpkfVQCLAFLGNGDVL-TGDSGGVMLIWSKTTveptpgkgpkgvYQISKQIKAHDGSVFTLCQMRNGMLLTGGGKDRK 543
Cdd:COG2319   249 -----VRSVAFSPDGRLLaSGSADGTVRLWDLAT------------GELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGT 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 544 IILWDhdLNPEREI-EVPDQYGTIRAVA---EGKadQFLVGTSRNFILRGTFNDGFQIEV-QGHTDELWGLATHPFKDLL 618
Cdd:COG2319   312 VRLWD--LATGKLLrTLTGHTGAVRSVAfspDGK--TLASGSDDGTVRLWDLATGELLRTlTGHTGAVTSVAFSPDGRTL 387

                         330
                  ....*....|...
gi 2462571909 619 LTCAQDRQVCLWN 631
Cdd:COG2319   388 ASGSADGTVRLWD 400
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 414-713 6.06e-18

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: 85.08  E-value: 6.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 414 AEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTWSGNSLTRKQgifgkYEKPKFVQCLAFLGNGD-VLTGDSGGVML 491
Cdd:cd00200     3 RTLKGHTGGVTCVAFSP-DGKLLATGSGDGtIKVWDLETGELLRTL-----KGHTGPVRDVAASADGTyLASGSSDKTIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 492 IWSKTTVEPTpgkgpkgvyqisKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDlNPEREIEVPDQYGTIRAVAE 571
Cdd:cd00200    77 LWDLETGECV------------RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGHTDWVNSVAF 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 572 GKADQFLVGTS----------RNFILRGTFNdgfqievqGHTDELWGLATHPFKDLLLTCAQDRQVCLWN-SMEHRLEWT 640
Cdd:cd00200   144 SPDGTFVASSSqdgtiklwdlRTGKCVATLT--------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDlSTGKCLGTL 215

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462571909 641 RLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLY 713
Cdd:cd00200   216 RGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 305-631 2.63e-17

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: 83.15  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 305 LFNYEERTQRHYL-GHTDCVKCLAIHPDKIRIATGqiaGVDKDgrplqphVRVWDSVTLSTLQIigLGTFERGVGCLDFS 383
Cdd:cd00200    35 VWDLETGELLRTLkGHTGPVRDVAASADGTYLASG---SSDKT-------IRLWDLETGECVRT--LTGHTSYVSSVAFS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 384 KaDSGVHLCVIDDSNehmLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTdaNTIITCGKS--HIFFWtwSGNSLTRKQGIF 461
Cdd:cd00200   103 P-DGRILSSSSRDKT---IKVWDVETGKCLTTLRGHTDWVNSVAFSPD--GTFVASSSQdgTIKLW--DLRTGKCVATLT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 462 GKYekpKFVQCLAFLGNG-DVLTGDSGGVMLIWSKTTVeptpgkgpkgvyQISKQIKAHDGSVFTLCQMRNGMLLTGGGK 540
Cdd:cd00200   175 GHT---GEVNSVAFSPDGeKLLSSSSDGTIKLWDLSTG------------KCLGTLRGHENGVNSVAFSPDGYLLASGSE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 541 DRKIILWDhdlnpereievpdqygtiravaegkadqflvgtSRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLT 620
Cdd:cd00200   240 DGTIRVWD---------------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLAS 278

                         330
                  ....*....|.
gi 2462571909 621 CAQDRQVCLWN 631
Cdd:cd00200   279 GSADGTIRIWD 289
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 18-61 1.92e-16

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


Pssm-ID: 409267  Cd Length: 44  Bit Score: 73.34  E-value: 1.92e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462571909  18 SDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVAS 61
Cdd:cd21931     1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 19-64 1.47e-14

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: 68.31  E-value: 1.47e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462571909  19 DVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21948     2 EVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRK 47
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 14-58 5.53e-12

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


Pssm-ID: 409270  Cd Length: 48  Bit Score: 60.81  E-value: 5.53e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462571909  14 AASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDH 58
Cdd:cd21949     1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 638-762 6.89e-06

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: 46.59  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909 638 EWTRLVDEPGHCAD--FHPSGTVVAIGT-HSGRW--FVLDAETRDLVSIHTDGNEQLSVmRYSIDGTFLAVGSH-DNFIY 711
Cdd:COG0823    22 EPRRLTNSPGIDTSpaWSPDGRRIAFTSdRGGGPqiYVVDADGGEPRRLTFGGGYNASP-SWSPDGKRLAFVSRsDGRFD 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462571909 712 LYVVSENGRKYSRYGRCTGHSSyithldWSPDNKYIM--SNSGDYEILYLYGL 762
Cdd:COG0823   101 IYVLDLDGGAPRRLTDGPGSPS------WSPDGRRIVfsSDRGGRPDLYVVDL 147
WD40 pfam00400
WD domain, G-beta repeat;
600-631 1.40e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.40e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462571909 600 QGHTDELWGLATHPFKDLLLTCAQDRQVCLWN 631
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 600-631 1.65e-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: 36.91  E-value: 1.65e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462571909  600 QGHTDELWGLATHPFKDLLLTCAQDRQVCLWN 631
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 638-762 1.89e-03

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


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 41.95  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462571909  638 EWTRLVDEPGHcADFHPS-----GTVVAIGTHSGRW--FVLDAETRDLVSIHTDGNeqlSVMRYSI----DGTFLAVGSH 706
Cdd:COG4946    333 PTRNLTNTPGV-RERLPAwspdgKSIAYFSDASGEYelYIAPADGSGEPKQLTLGD---LGRVFNPvwspDGKKIAFTDN 408

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462571909  707 DNFIYLY-VVSENGRK--YSRYGrctghsSYITHLDWSPDNKYI---MSNSGDYEILYLYGL 762
Cdd:COG4946    409 RGRLWVVdLASGKVRKvdTDGYG------DGISDLAWSPDSKWLaysKPGPNQLSQIFLYDV 464
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 728-753 4.77e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.37  E-value: 4.77e-03
                           10        20
                   ....*....|....*....|....*.
gi 2462571909  728 CTGHSSYITHLDWSPDNKYIMSNSGD 753
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDD 33
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 318-358 9.05e-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: 9.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2462571909  318 GHTDCVKCLAIHPDKIRIATGqiagvDKDGrplqpHVRVWD 358
Cdd:smart00320  10 GHTGPVTSVAFSPDGKYLASG-----SDDG-----TIKLWD 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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