Most partial domains in proteins are alignment and annotation artifacts

Genome Biology

Volumn 16, Issue 1, 2015, Pages

  Triant, Deborah A ^a   Pearson, William R ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDES AND PROTEINS; PFAM PROTEIN; PFAM27 PROTEIN; PFAMA PROTEIN; UNCLASSIFIED DRUG; PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DROSOPHILA; HUMAN; MOUSE; NONHUMAN; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DATABASE; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; SEQUENCE ANALYSIS; STRUCTURAL HOMOLOGY; STRUCTURE ANALYSIS; ANIMAL; CHEMISTRY; GENETIC DATABASE; GENETICS; MOLECULAR GENETICS; MOLECULAR MODEL; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SOFTWARE;

EUKARYOTA;

ANIMALS; DATABASES, GENETIC; DATABASES, PROTEIN; DROSOPHILA; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE ANNOTATION; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SEQUENCE ALIGNMENT; SOFTWARE;

EID: 84939207424     PISSN: 14747596     EISSN: 1474760X     Source Type: Journal    
DOI: 10.1186/s13059-015-0656-7     Document Type: Article

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