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The YARHG Domain: An Extracellular Domain in Search of a Function

We have identified a new bacterial protein domain that we hypothesise binds to peptidoglycan. This domain is called the YARHG domain after the most highly conserved sequence-segment. The domain is found in the extracellular space and is likely to be composed of four alpha-helices. The domain is foun...

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Detalles Bibliográficos
Autores principales: Coggill, Penny, Bateman, Alex
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3355149/
https://www.ncbi.nlm.nih.gov/pubmed/22615736
http://dx.doi.org/10.1371/journal.pone.0035575
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author Coggill, Penny
Bateman, Alex
author_facet Coggill, Penny
Bateman, Alex
author_sort Coggill, Penny
collection PubMed
description We have identified a new bacterial protein domain that we hypothesise binds to peptidoglycan. This domain is called the YARHG domain after the most highly conserved sequence-segment. The domain is found in the extracellular space and is likely to be composed of four alpha-helices. The domain is found associated with protein kinase domains, suggesting it is associated with signalling in some bacteria. The domain is also found associated with three different families of peptidases. The large number of different domains that are found associated with YARHG suggests that it is a useful functional module that nature has recombined multiple times.
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spelling pubmed-33551492012-05-21 The YARHG Domain: An Extracellular Domain in Search of a Function Coggill, Penny Bateman, Alex PLoS One Research Article We have identified a new bacterial protein domain that we hypothesise binds to peptidoglycan. This domain is called the YARHG domain after the most highly conserved sequence-segment. The domain is found in the extracellular space and is likely to be composed of four alpha-helices. The domain is found associated with protein kinase domains, suggesting it is associated with signalling in some bacteria. The domain is also found associated with three different families of peptidases. The large number of different domains that are found associated with YARHG suggests that it is a useful functional module that nature has recombined multiple times. Public Library of Science 2012-05-17 /pmc/articles/PMC3355149/ /pubmed/22615736 http://dx.doi.org/10.1371/journal.pone.0035575 Text en Coggill, Bateman. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Coggill, Penny
Bateman, Alex
The YARHG Domain: An Extracellular Domain in Search of a Function
title The YARHG Domain: An Extracellular Domain in Search of a Function
title_full The YARHG Domain: An Extracellular Domain in Search of a Function
title_fullStr The YARHG Domain: An Extracellular Domain in Search of a Function
title_full_unstemmed The YARHG Domain: An Extracellular Domain in Search of a Function
title_short The YARHG Domain: An Extracellular Domain in Search of a Function
title_sort yarhg domain: an extracellular domain in search of a function
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3355149/
https://www.ncbi.nlm.nih.gov/pubmed/22615736
http://dx.doi.org/10.1371/journal.pone.0035575
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