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399  structures 5116  species 6  interactions 30822  sequences 174  architectures

Clan: FAD_DHS (CL0085)

Summary

DHS-like NAD/FAD-binding domain Add an annotation

The members of this family adopt a Rossmann fold, similar to CLAN:CL0063. However, the members of this family are distinguished in that the FAD/NAD cofactor is bound in the opposite direction. In this arrangement, the adenosine moiety is found bound at the second half of the fold. In addition, the conserved GxGxxG motif found in classical NADP binding Rossmann folds is absent. Finally, another distinguishing characteristic is the formation of an internal hydrogen bond in the FAD molecule [1].

This clan contains 7 families and the total number of domains in the clan is 30822. The clan was built by RD Finn.

Literature references

  1. Dym O, Eisenberg D; , Protein Sci 2001;10:1712-1728.: Sequence-structure analysis of FAD-containing proteins. PUBMED:11514662 EPMC:11514662

Members

This clan contains the following 7 member families:

CO_dh DS ETF_alpha PNTB SIR2 SIR2_2 TPP_enzyme_M

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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Alignments

The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
TPP_enzyme_M (PF00205) 15120 (49.1%) View
SIR2 (PF02146) 5869 (19.0%) View
ETF_alpha (PF00766) 4727 (15.3%) View
PNTB (PF02233) 2429 (7.9%) View
SIR2_2 (PF13289) 1624 (5.3%) View
DS (PF01916) 956 (3.1%) View
CO_dh (PF02552) 97 (0.3%) View
Total: 7 Total: 30822 Clan alignment
 

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Family relationships

This diagram shows the relationships between members of this clan. More...

Species distribution

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This tree shows the occurrence of the domains in this clan across different species. More...

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Interactions

There are 6 interactions for this clan. More...

Interacting families
A B
TPP_enzyme_M TPP_enzyme_M
TPP_enzyme_C
TPP_enzyme_N
SIR2 SIR2
DS DS
ETF_alpha ETF

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.

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