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{{Short description|Biological database}}
{{infobox biodatabase
|title = CDD
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|laboratory =
|author = Aron Marchler-Bauer
|
|released = 2003
|standard =
|format =
|url =
|download =
|webservice =
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}}
The '''Conserved Domain Database''' ('''CDD''') is a database of well-annotated [[multiple sequence alignment]] models and derived database search models, for ancient [[Protein ___domain|domains]] and full-length proteins.<ref name="
| last1 = Marchler-Bauer | first1 = A.
| last2 = Zheng | first2 = C.
| last3 = Chitsaz | first3 = F.
| last4 = Derbyshire | first4 = M. K.
| last5 = Geer | first5 = L. Y.
| last6 = Geer | first6 = R. C.
| last7 = Gonzales | first7 = N. R.
| last8 = Gwadz | first8 = M.
| last9 = Hurwitz | first9 = D. I.
| last10 = Lanczycki
| doi = 10.1093/nar/gks1243 | first10 = C. J.
| last11 = Lu | first11 = F.
| last12 = Lu | first12 = S.
| last13 = Marchler | first13 = G. H.
| last14 = Song | first14 = J. S.
| last15 = Thanki | first15 = N.
| last16 = Yamashita | first16 = R. A.
| last17 = Zhang | first17 = D.
| last18 = Bryant | first18 = S. H.
| title = CDD: Conserved domains and protein three-dimensional structure
| journal = Nucleic Acids Research
| volume = 41
| issue = Database issue
| pages = D348–D352
| year = 2012
| pmid = 23197659
| pmc =3531192
}}</ref> The database consists of position-specific score matrices and serves as resource for protein annotation such as identification of conserved ___domain or inference of functional site.<ref>{{Cite journal |last=Marchler-Bauer |first=Aron |last2=Lu |first2=Shennan |last3=Anderson |first3=John B. |last4=Chitsaz |first4=Farideh |last5=Derbyshire |first5=Myra K. |last6=DeWeese-Scott |first6=Carol |last7=Fong |first7=Jessica H. |last8=Geer |first8=Lewis Y. |last9=Geer |first9=Renata C. |last10=Gonzales |first10=Noreen R. |last11=Gwadz |first11=Marc |last12=Hurwitz |first12=David I. |last13=Jackson |first13=John D. |last14=Ke |first14=Zhaoxi |last15=Lanczycki |first15=Christopher J. |date=2011-01-01 |title=CDD: a Conserved Domain Database for the functional annotation of proteins |url=https://academic.oup.com/nar/article/39/suppl_1/D225/2507607 |journal=Nucleic Acids Research |volume=39 |issue=suppl_1 |pages=D225–D229 |doi=10.1093/nar/gkq1189 |issn=0305-1048|pmc=3013737 }}</ref>
==Philosophy==
Domains can be thought of as distinct functional and/or structural units of a protein. These two classifications coincide rather often, as a matter of fact, and what is found as an independently folding unit of a polypeptide chain also carries specific function. Domains are often identified as recurring (sequence or structure) units, which may exist in various contexts. In [[molecular evolution]] such domains may have been utilized as building blocks, and may have been recombined in different arrangements to modulate protein function. CDD defines conserved domains as recurring units in molecular evolution, the extents of which can be determined by sequence and structure analysis.
The goal of the NCBI conserved ___domain curation project is to provide database users with insights into how patterns of residue conservation and divergence in a family relate to functional properties, and to provide useful links to more detailed information that may help to understand those sequence/structure/function relationships. To do this, CDD Curators include the following types of information in order to supplement and enrich the traditional multiple sequence alignments that form the foundation of ___domain models: 3-dimensional structures and conserved core motifs, conserved features/sites, phylogenetic organization, links to electronic literature resources.
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==Searching the database==
The collection is also part of
==References==
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==External links==
* {{cite web | url =
[[Category:
[[Category:Protein structure]]
[[Category:Protein domains]]
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