CpcD-like domain (IPR008213)

Short name: CpcD-like_dom

Overlapping homologous superfamilies

Domain relationships



Ferredoxin-NADP(+) oxydoreductase (FNR) (EC: transfers electrons from ferredoxin (or flavodoxin) to NADP(+) to generate NADPH. In eucaryotes, the nuclear-encoded, chloroplast-targeted enzyme contains two domains: an FAD-binding domain (see PDOC51384) and an NADP(+)-binding domain. With the exception of Gloeobacter violaceus PCC 7421, the predicted sequences of all cyanobacterial petH genes, encoding FNR, correspond to a protein containing three domains. Two domains at the C terminus correspond to the FAD- and NADP(+)-binding domains of higher plants FNR protein, which compose the catalytic domains of the enzyme. The N-terminal domain is similar to phycobilisome (PBS)-associated linker proteins from numerous cyanobacteria [PMID: 1554697, PMID: 2040095, PMID: 4636046] and is associated with:

  • - CpcD, the phycocyanin (PC)-associated, rod-capping, linker polypeptide of PBS. The similarity spans nearly the entire sequence of this linker class.
  • - CpcC, the PC-associated rod linker polypeptide. The similarity is confined only to the C terminus of this linker class.
  • - ApcC, the allophycocyanin (APC)-associated, core linker polypeptide. The similarity only correspond to about half of the molecule.

The CpcD-like domain has an elongated shape and consists of a three-stranded beta-sheet, two alpha-helices, one of which has only about one turn, and the connecting random coil segments [PMID: 9990029].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

No terms assigned in this category.

Cellular Component

GO:0030089 phycobilisome

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles