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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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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. |
format | Online Article Text |
id | pubmed-3355149 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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