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Provides automatic classification and functional annotation of protein sequences based on their homology to characterized templates. HAMAP is based on a collection of expert curated protein family profiles, that are used to determine family membership of protein sequences, and annotation rules. This resource contains more than 200 family profiles and 270 annotation rules. These annotations can be accessed via UniProtKB, or generated by users for their own protein or proteome sequences via the HAMAP-Scan service on the HAMAP website.
Stores annotations and structures for protein pre-, co- and post-translational modifications including amino-terminal, carboxyl-terminal and peptide chain cross-link modifications. RESID provides information such as dates for database entry and modification, systematic name and Chemical Abstracts Service registry number, alternate names, atomic formula and mass, enzyme activities; indicators for amino-terminal, carboxyl-terminal or peptide chain cross-link modifications; literature citations, keywords and feature table representations for the modification in the Protein Information Resource (PIR) and SWISS-PROT protein sequence databases.
Provides access to the result of repeat protein domains, obtained from the amplification of population-genetic signal by constructing a motif-based multiple sequence alignment (motif-MSA). Intensification is a resource for annotating variants in 12 protein-protein interactions (PPI) repeat protein domains (RPDs). The database contains data files for ankyrins (ANK), annexins (ANX), armadillos (ARM), cadherin repeats (CA), fibronectin type 2 domains (FN2), fibronectin type 3 domains (FN3), leucine-rich repeats (LRR_TYP), spectrin repeats (SPEC), tetratricopeptide repeats (TPR), ubiquitin-interacting motifs (UIM), WD40 repeats (WD40), and WW domains (WW).
SInCRe / Structural Interactome Computational Resource
An integrated database for Mycobacterium tuberculosis H37Rv (Mtb) that collates information on protein sequences, domain assignments, functional annotation and 3D structural information along with protein-protein and protein-small molecule interactions. The motivation for development of this database is to provide an integrated platform to allow easily access and interpretation of data and results obtained by all the groups in CamBan in the field of Mtb informatics.
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