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Homology modeling and assigned functional annotation of an uncharacterized antitoxin protein from Streptomyces xinghaiensis.


ABSTRACT: Streptomyces xinghaiensis is a Gram-positive, aerobic and non-motile bacterium. The bacterial genome is known. Therefore, it is of interest to study the uncharacterized proteins in the genome. An uncharacterized protein (gi|518540893|86 residues) in the genome was selected for a comprehensive computational sequence-structure-function analysis using available data and tools. Subcellular localization of the targeted protein with conserved residues and assigned secondary structures is documented. Sequence homology search against the protein data bank (PDB) and non-redundant GenBank proteins using BLASTp showed different homologous proteins with known antitoxin function. A homology model of the target protein was developed using a known template (PDB ID: 3CTO:A) with 62% sequence similarity in HHpred after assessment using programs PROCHECK and QMEAN6. The predicted active site using CASTp is analyzed for assigned anti-toxin function. This information finds specific utility in annotating the said uncharacterized protein in the bacterial genome.

SUBMITTER: Oany AR 

PROVIDER: S-EPMC4748018 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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Homology modeling and assigned functional annotation of an uncharacterized antitoxin protein from Streptomyces xinghaiensis.

Oany Arafat Rahman AR   Ahmed Md Shahabuddin MS   Jahan Nasreen N   Latif Md Abdul MA   Mahmud Shahin S   Hossain Md Ahmed MA   Akter Fatema F   Rakib Hasibul Haque HH   Islam Md Shariful MS  

Bioinformation 20151130 11


Streptomyces xinghaiensis is a Gram-positive, aerobic and non-motile bacterium. The bacterial genome is known. Therefore, it is of interest to study the uncharacterized proteins in the genome. An uncharacterized protein (gi|518540893|86 residues) in the genome was selected for a comprehensive computational sequence-structure-function analysis using available data and tools. Subcellular localization of the targeted protein with conserved residues and assigned secondary structures is documented. S  ...[more]

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