Review




Structured Review

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
90/100 stars

Images

1) Product Images from "Caenorhabditis elegans β-G Spectrin Is Dispensable for Establishment of Epithelial Polarity, but Essential for Muscular and Neuronal Function"

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

Journal: The Journal of Cell Biology

doi:

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.
Figure Legend 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.

Techniques Used: Software



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