sequence alignment programs sequencher Search Results


geneworks v2.5.1  (GeneWorks)
90
GeneWorks geneworks v2.5.1
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Geneworks V2.5.1, supplied by GeneWorks, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/pmc02174577-60-6-5?v=GeneWorks
Average 90 stars, based on 1 article reviews
geneworks v2.5.1 - by Bioz Stars, 2026-08
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sequence data visualization tools  (Celera)
90
Celera sequence data visualization tools
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Sequence Data Visualization Tools, supplied by Celera, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/pmc03134613-1734-19-9?v=Celera
Average 90 stars, based on 1 article reviews
sequence data visualization tools - by Bioz Stars, 2026-08
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transcript assemblertm software  (Paracel BLAST)
90
Paracel BLAST transcript assemblertm software
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Transcript Assemblertm Software, supplied by Paracel BLAST, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/us08716023-469-5-8?v=Paracel+BLAST
Average 90 stars, based on 1 article reviews
transcript assemblertm software - by Bioz Stars, 2026-08
90/100 stars
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vector nt  (InforMax Inc)
90
InforMax Inc vector nt
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Vector Nt, supplied by InforMax Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/pm15607004-54-5-7?v=InforMax+Inc
Average 90 stars, based on 1 article reviews
vector nt - by Bioz Stars, 2026-08
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codoncode aligner  (CodonCode corporation)
90
CodonCode corporation codoncode aligner
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Codoncode Aligner, supplied by CodonCode corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/10__1016_slash_j__jevs__2018__08__010-67-8-10?v=CodonCode+corporation
Average 90 stars, based on 1 article reviews
codoncode aligner - by Bioz Stars, 2026-08
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dnaman v6.0.3.99 software  (Lynnon corporation)
90
Lynnon corporation dnaman v6.0.3.99 software
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Dnaman V6.0.3.99 Software, supplied by Lynnon corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/pmc10648341-147-12-15?v=Lynnon+corporation
Average 90 stars, based on 1 article reviews
dnaman v6.0.3.99 software - by Bioz Stars, 2026-08
90/100 stars
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clustalw program  (MacVector inc)
90
MacVector inc clustalw program
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Clustalw Program, supplied by MacVector inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/10__1042_slash_bj3470763-146-5-8?v=MacVector+inc
Average 90 stars, based on 1 article reviews
clustalw program - by Bioz Stars, 2026-08
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sequence alignments  (MacVector inc)
90
MacVector inc sequence alignments
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Sequence Alignments, supplied by MacVector inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/10__1128_slash_jb__01031___09-121-2-8?v=MacVector+inc
Average 90 stars, based on 1 article reviews
sequence alignments - by Bioz Stars, 2026-08
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clustalw function of macvector version 12.0  (MacVector inc)
90
MacVector inc clustalw function of macvector version 12.0
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Clustalw Function Of Macvector Version 12.0, supplied by MacVector inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/10__1007_slash_s10658___013___0179___6-153-11-13?v=MacVector+inc
Average 90 stars, based on 1 article reviews
clustalw function of macvector version 12.0 - by Bioz Stars, 2026-08
90/100 stars
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dnaman  (Lynnon corporation)
90
Lynnon corporation dnaman
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Dnaman, supplied by Lynnon corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/pm34074728-104-8-9?v=Lynnon+corporation
Average 90 stars, based on 1 article reviews
dnaman - by Bioz Stars, 2026-08
90/100 stars
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macvector 9.0.2 software  (MacVector inc)
90
MacVector inc macvector 9.0.2 software
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Macvector 9.0.2 Software, supplied by MacVector inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/pm18568656-95-7-9?v=MacVector+inc
Average 90 stars, based on 1 article reviews
macvector 9.0.2 software - by Bioz Stars, 2026-08
90/100 stars
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clustalw  (MacVector inc)
90
MacVector inc clustalw
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Clustalw, supplied by MacVector inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sequence+alignment+programs+sequencher/10__1074_slash_jbc__m109060200-144-49-54?v=MacVector+inc
Average 90 stars, based on 1 article reviews
clustalw - by Bioz Stars, 2026-08
90/100 stars
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Image Search Results


Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks v2.5.1 software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.

Journal: The Journal of Cell Biology

Article Title: Caenorhabditis elegans β-G Spectrin Is Dispensable for Establishment of Epithelial Polarity, but Essential for Muscular and Neuronal Function

doi:

Figure Lengend Snippet: Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks v2.5.1 software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.

Article Snippet: Sequence alignments were made using Geneworks v2.5.1.

Techniques: Software