Domain Annotation

Domain Annotation

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CD Genomics is able to help customers achieve rapid identification and annotation of protein structural domains using a variety of tools to shorten the pre-study time for researchers.

Introduction of Domain Annotation

Structural domains are evolutionarily conserved sequence units of proteins, which are standard components of protein structure and function and carry many features, including catalytic activity, substrate binding, and structural features. A structural domain may also have multiple copies in a protein, and the same structural domain may be in different positions in different proteins. Identification of interacting structural domains is important for understanding protein-protein interactions. A rich and increasingly updated database of structural domain interactions has been generated, relying on further mining of experimental data and computational prediction of a variety of different input data. Protein structural domain annotation relies on these databases to help scientists advance their research.

BRCA1 variant functional annotationFigure 1. BRCA1 variant functional annotation. (Fernandes VC, et al., 2019)

Application Field

Domain annotation services can be used for but are not limited to the following research:

  • For prediction of protein interactions.
  • For assessing the plausibility of large-scale protein-protein interactions.
  • Used for pathway studies.

CD Genomics Domain Annotation Service Pipeline

CD Genomics Domain Annotation Service Pipeline

Domain Annotation Service Content

We are able to integrate resources from multiple databases to provide professional protein structural domain annotation services based on protein family, protein classification, and other data. We can provide structural domain annotation services based on the following database resources.

3D interacting domains 3DID collects DDI of proteins with known high-resolution 3D structures.
Protein families database Pfam is a large comprehensive database of protein families and structural domains based on sequence multiplexing and Hidden Markov Models.
Database of interacting domains The InterDom database is a protein DDI database computationally extrapolated from multiple data sources.
Domain interaction map DIMA mainly provides analysis and annotation of proteins from the whole genome.
Database of protein domain interactions DOMINE is a database of known and predicted protein DDI.
InterProScan protein sequence analysis & classification InterPro is a comprehensive database that can be used for the annotation of proteins and protein signal peptides.
Conserved domain database CDD collected multiplexed comparative sequence models as well as full-length protein sequences to construct conserved structural domains.
Simple modular architecture research tool SMART can be used for automated identification and annotation of protein structural domains.

We are able to use domain annotation services to help our customers achieve high throughput data analysis in genomics and proteomics. For questions about analysis content, project cycle, and pricing, please click online inquiry.

How It Works

CD Genomics is a professional bioinformatics service provider with years of experience in NGS and long-read sequencing (PacBio SMRT and Oxford Nanopore platforms) data, proteomics and metabolomics data analysis, integrated analysis services, database construction, and other bioinformatics solutions.

How It Works

CD Genomics has professional bioinformatics experts who have successfully provided domain annotation services to researchers in many different fields. Our professional skills and enthusiasm will provide you with high-quality analysis services. If you are interested in our services, please contact us for more details.


  1. Fernandes VC, et al. Impact of amino acid substitutions at secondary structures in the BRCT domains of the tumor suppressor BRCA1: Implications for clinical annotation. J Biol Chem. 2019 Apr 12; 294(15): 5980-5992.
* For Research Use Only. Not for use in diagnostic procedures.
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