Cupin superfamily

Cupin superfamily
Cupin_1
PDB 1l3j EBI.jpg
crystal structure of oxalate decarboxylase formate complex
Identifiers
Symbol Cupin_1
Pfam PF00190
Pfam clan CL0029
InterPro IPR006045
SCOP 2phl
Cupin_2
PDB 1y3t EBI.jpg
crystal structure of yxag, a dioxygenase from bacillus subtilis
Identifiers
Symbol Cupin_2
Pfam PF07883
Pfam clan CL0029
InterPro IPR013096
SCOP 1vj2
Cupin_3
PDB 1rc6 EBI.jpg
crystal structure of protein ylba from e. coli, pfam duf861
Identifiers
Symbol Cupin_3
Pfam PF05899
Pfam clan CL0029
InterPro IPR008579
SCOP 1o5u
Cupin_4
Identifiers
Symbol Cupin_4
Pfam PF08007
Pfam clan CL0029
Cupin_5
PDB 1yud EBI.jpg
x-ray crystal structure of protein so0799 from shewanella oneidensis. northeast structural genomics consortium target sor12.
Identifiers
Symbol Cupin_5
Pfam PF06172
Pfam clan CL0029
InterPro IPR009327
Cupin_6
Identifiers
Symbol Cupin_6
Pfam PF12852
Pfam clan CL0029
Cupin_7
Identifiers
Symbol Cupin_7
Pfam PF12973
Pfam clan CL0029

In molecular biology, the cupin superfamily of proteins is a diverse superfamily of proteins containing a conserved barrel domain, cupa is the Latin term for a small barrel. The cupin superfamily includes a wide variety of enzymes, but notably contains the non-enzymatic seed storage proteins also.[1][2]

References

  1. ^ Dunwell JM (1998). "Cupins: a new superfamily of functionally diverse proteins that include germins and plant storage proteins". Biotechnol. Genet. Eng. Rev. 15: 1–32. PMID 9573603. 
  2. ^ Dunwell, J. M.; Purvis, A.; Khuri, S. (2004). "Cupins: The most functionally diverse protein superfamily?". Phytochemistry 65 (1): 7–17. doi:10.1016/j.phytochem.2003.08.016. PMID 14697267.  edit

This article includes text from the public domain Pfam and InterPro IPR013096

This article includes text from the public domain Pfam and InterPro IPR006045

This article includes text from the public domain Pfam and InterPro IPR009327

This article includes text from the public domain Pfam and InterPro IPR008579


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