Your browser doesn't support javascript.
loading
CDD: specific functional annotation with the Conserved Domain Database.
Marchler-Bauer, Aron; Anderson, John B; Chitsaz, Farideh; Derbyshire, Myra K; DeWeese-Scott, Carol; Fong, Jessica H; Geer, Lewis Y; Geer, Renata C; Gonzales, Noreen R; Gwadz, Marc; He, Siqian; Hurwitz, David I; Jackson, John D; Ke, Zhaoxi; Lanczycki, Christopher J; Liebert, Cynthia A; Liu, Chunlei; Lu, Fu; Lu, Shennan; Marchler, Gabriele H; Mullokandov, Mikhail; Song, James S; Tasneem, Asba; Thanki, Narmada; Yamashita, Roxanne A; Zhang, Dachuan; Zhang, Naigong; Bryant, Stephen H.
Afiliação
  • Marchler-Bauer A; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bldg. 38 A, Room 8N805, 8600 Rockville Pike, Bethesda, MD 20894, USA. bauer@ncbi.nlm.nih.gov
Nucleic Acids Res ; 37(Database issue): D205-10, 2009 Jan.
Article em En | MEDLINE | ID: mdl-18984618
NCBI's Conserved Domain Database (CDD) is a collection of multiple sequence alignments and derived database search models, which represent protein domains conserved in molecular evolution. The collection can be accessed at http://www.ncbi.nlm.nih.gov/Structure/cdd/cdd.shtml, and is also part of NCBI's Entrez query and retrieval system, cross-linked to numerous other resources. CDD provides annotation of domain footprints and conserved functional sites on protein sequences. Precalculated domain annotation can be retrieved for protein sequences tracked in NCBI's Entrez system, and CDD's collection of models can be queried with novel protein sequences via the CD-Search service at http://www.ncbi.nlm.nih.gov/Structure/cdd/wrpsb.cgi. Starting with the latest version of CDD, v2.14, information from redundant and homologous domain models is summarized at a superfamily level, and domain annotation on proteins is flagged as either 'specific' (identifying molecular function with high confidence) or as 'non-specific' (identifying superfamily membership only).
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Estrutura Terciária de Proteína / Bases de Dados de Proteínas Idioma: En Revista: Nucleic Acids Res Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Estrutura Terciária de Proteína / Bases de Dados de Proteínas Idioma: En Revista: Nucleic Acids Res Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Estados Unidos