E1DS: catalytic site prediction based on 1D signatures of concurrent conservation.
Large-scale automatic annotation of protein sequences remains challenging in postgenomics era. E1DS is designed for annotating enzyme sequences based on a repository of 1D signatures. The employed sequence signatures are derived using a novel pattern mining approach that discovers long motifs consisted of several sequential blocks (conserved segments). Each of the sequential blocks is considerably conserved among the protein members of an EC group. Moreover, a signature includes at least three sequential blocks that are concurrently conserved, i.e. frequently observed together in sequences. In other words, a sequence signature is consisted of residues from multiple regions of the protein sequence, which echoes the observation that an enzyme catalytic site is usually constituted of residues that are largely separated in the sequence. E1DS currently contains 5421 sequence signatures that in total cover 932 4-digital EC numbers. E1DS is evaluated based on a collection of enzymes with catalytic sites annotated in Catalytic Site Atlas. When compared to the famous pattern database PROSITE, predictions based on E1DS signatures are considered more sensitive in identifying catalytic sites and the involved residues. E1DS is available at http://e1ds.ee.ncku.edu.tw/ and a mirror site can be found at http://e1ds.csbb.ntu.edu.tw/.
Chien
Ting-Ying
TY
Department of Computer Science and Information Engineering, National Taiwan University, Taipei, Taiwan, ROC.
Chang
Darby Tien-Hao
DT
Chen
Chien-Yu
CY
Weng
Yi-Zhong
YZ
Hsu
Chen-Ming
CM
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D017124:Conserved Sequence; D004798:Enzymes / Q000737:chemistry*; D020407:Internet; D020539:Sequence Analysis, Protein; D012984:Software; D014584:User-Computer Interface
D004798:Enzymes