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echinoderm microtubule-associated protein-like 1 isoform X4 [Latimeria chalumnae]
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||||
HELP | pfam03451 | HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
197-268 | 4.59e-40 | ||||||
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons. : Pssm-ID: 460922 Cd Length: 72 Bit Score: 141.54 E-value: 4.59e-40
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TD_EMAP1 | cd21947 | trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ... |
22-79 | 1.40e-37 | ||||||
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm microtubule-associated protein-like 1 (EMAP-1), also called EMAL1, EMAPL, or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. This model corresponds to a conserved region located at the N-terminus of EMAP-1, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-4 and EMAP-2. : Pssm-ID: 409268 Cd Length: 58 Bit Score: 134.08 E-value: 1.40e-37
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
357-708 | 1.05e-29 | ||||||
WD40 repeat [General function prediction only]; : Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 122.33 E-value: 1.05e-29
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WD40 super family | cl29593 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
679-824 | 7.50e-08 | ||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. The actual alignment was detected with superfamily member cd00200: Pssm-ID: 475233 [Multi-domain] Cd Length: 289 Bit Score: 54.65 E-value: 7.50e-08
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
271-318 | 2.61e-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: 36.14 E-value: 2.61e-03
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Name | Accession | Description | Interval | E-value | |||||||
HELP | pfam03451 | HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
197-268 | 4.59e-40 | |||||||
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons. Pssm-ID: 460922 Cd Length: 72 Bit Score: 141.54 E-value: 4.59e-40
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TD_EMAP1 | cd21947 | trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ... |
22-79 | 1.40e-37 | |||||||
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm microtubule-associated protein-like 1 (EMAP-1), also called EMAL1, EMAPL, or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. This model corresponds to a conserved region located at the N-terminus of EMAP-1, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-4 and EMAP-2. Pssm-ID: 409268 Cd Length: 58 Bit Score: 134.08 E-value: 1.40e-37
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
357-708 | 1.05e-29 | |||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 122.33 E-value: 1.05e-29
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
274-708 | 1.55e-24 | |||||||
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: 104.34 E-value: 1.55e-24
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
679-824 | 7.50e-08 | |||||||
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: 54.65 E-value: 7.50e-08
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ANAPC4_WD40 | pfam12894 | Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
603-692 | 2.73e-04 | |||||||
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC, Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 40.72 E-value: 2.73e-04
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
271-318 | 2.61e-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: 36.14 E-value: 2.61e-03
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WD40 | pfam00400 | WD domain, G-beta repeat; |
271-318 | 3.01e-03 | |||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.17 E-value: 3.01e-03
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
549-580 | 7.00e-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: 7.00e-03
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Name | Accession | Description | Interval | E-value | |||||||
HELP | pfam03451 | HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
197-268 | 4.59e-40 | |||||||
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons. Pssm-ID: 460922 Cd Length: 72 Bit Score: 141.54 E-value: 4.59e-40
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TD_EMAP1 | cd21947 | trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ... |
22-79 | 1.40e-37 | |||||||
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm microtubule-associated protein-like 1 (EMAP-1), also called EMAL1, EMAPL, or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. This model corresponds to a conserved region located at the N-terminus of EMAP-1, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-4 and EMAP-2. Pssm-ID: 409268 Cd Length: 58 Bit Score: 134.08 E-value: 1.40e-37
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
357-708 | 1.05e-29 | |||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 122.33 E-value: 1.05e-29
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
262-665 | 6.89e-27 | |||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.85 E-value: 6.89e-27
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
353-823 | 7.44e-26 | |||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 110.77 E-value: 7.44e-26
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
263-583 | 3.55e-25 | |||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 108.85 E-value: 3.55e-25
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
274-708 | 1.55e-24 | |||||||
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: 104.34 E-value: 1.55e-24
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WD40 | COG2319 | WD40 repeat [General function prediction only]; |
478-823 | 2.70e-22 | |||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 100.37 E-value: 2.70e-22
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TD_EMAP4 | cd21950 | trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ... |
20-74 | 2.56e-20 | |||||||
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm microtubule-associated protein-like 4 (EMAP-4), also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to the N-terminal trimerization domain of EMAP-4. Pssm-ID: 409271 Cd Length: 59 Bit Score: 85.04 E-value: 2.56e-20
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
549-822 | 4.45e-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: 91.24 E-value: 4.45e-20
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
265-580 | 9.89e-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: 90.47 E-value: 9.89e-20
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TD_EMAP2 | cd21948 | trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ... |
32-79 | 1.34e-18 | |||||||
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm microtubule-associated protein-like 2 (EMAP-2), also called EML2 or EMAPL2, is a tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. This model corresponds to the N-terminal trimerization domain of EMAP-2. Pssm-ID: 409269 Cd Length: 48 Bit Score: 79.87 E-value: 1.34e-18
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TD_EMAP-like | cd21931 | trimerization domain of the echinoderm microtubule-associated protein-like family; The ... |
32-74 | 1.28e-17 | |||||||
trimerization domain of the echinoderm microtubule-associated protein-like family; The echinoderm microtubule-associated protein (EMAP)-like (EML) family includes EMAP-1, EMAP-2, EMAP-3, and EMAP-4. EMAP-1, also called EMAL1, EMAPL or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. EMAP-2, also called EML2 or EMAPL2, is a tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. EMAP-3, also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. EMAP-4, also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved trimerization domain located at the N-terminus of EML family members. Pssm-ID: 409267 Cd Length: 44 Bit Score: 76.81 E-value: 1.28e-17
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TD_EMAP3 | cd21949 | trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ... |
28-72 | 1.14e-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: 60.04 E-value: 1.14e-11
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
549-821 | 3.35e-11 | |||||||
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: 65.05 E-value: 3.35e-11
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WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
679-824 | 7.50e-08 | |||||||
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: 54.65 E-value: 7.50e-08
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ANAPC4_WD40 | pfam12894 | Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
603-692 | 2.73e-04 | |||||||
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC, Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 40.72 E-value: 2.73e-04
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
271-318 | 2.61e-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: 36.14 E-value: 2.61e-03
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WD40 | pfam00400 | WD domain, G-beta repeat; |
271-318 | 3.01e-03 | |||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.17 E-value: 3.01e-03
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WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
549-580 | 7.00e-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: 7.00e-03
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WD40 | pfam00400 | WD domain, G-beta repeat; |
549-580 | 9.73e-03 | |||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 34.63 E-value: 9.73e-03
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Blast search parameters | ||||
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