Open AccessCHDL: A cadherin‐like domain in Proteobacteria and Cyanobacteria
Author(s) -
Cao Lihuan,
Yan Xiaomei,
Borysenko Christopher W.,
Blair Harry C.,
Wu Chaoqun,
Yu Long
Publication year - 2005
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/j.femsle.2005.08.004
Subject(s) - architecture domain , cadherin , biology , computational biology , cyanobacteria , immunoglobulin domain , domain (mathematical analysis) , computer science , biochemistry , genetics , gene , bacteria , mathematical analysis , mathematics , software architecture , software , enterprise architecture framework , cell , programming language
We identified a cadherin‐like domain (CHDL) using computational analysis. The CHDL domain is mostly distributed in Proteobacteria and Cyanobacteria, although it is also found in some eukaryotic proteins. Prediction of three‐dimensional protein folding indicated that the CHDL domain has an immunoglobulin β‐sandwich fold and belongs to the cadherin superfamily. The CHDL domain does not have LDRE and DxNDN motifs, which are conserved in the cadherin domain, but has three other motifs: PxAxxD, DxDxD and YT‐V/I‐S/T‐D, which might contribute to forming a calcium‐binding site. The identification of this cadherin‐like domain indicates that the cadherin superfamliy may exhibit wider sequence and structural diversity than previously appreciated. Domain architecture analysis revealed that the CHDL domain is also associated with other adhesion domains as well as enzyme domains. Based on computational analysis and previous experimental data, we predict that the CHDL domain has calcium‐binding and also carbohydrate‐binding activity.