Protein Family Models

This entry contains many divergent copper oxidase-like domains that are not recognised by the Pfam:PF00394 model. [1]. 2404764. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Messerschmidt A, Huber R;. Eur J Biochem 1990;187:341-352. [2]. 1548698. Refined crystal structure of ascorbate oxidase at 1.9 A resolution. Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano L, Petruzzelli R, Rossi A, Finazzi-Agro A;. J Mol Biol 1992;224:179-205. [3]. 10573417. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Page CC, Moser CC, Chen X, Dutton PL;. Nature 1999;402:47-52. [4]. 7599131. X-ray absorption studies and homology modeling define the structural features that specify the nature of the copper site in rusticyanin. Grossmann JG, Ingledew WJ, Harvey I, Strange RW, Hasnain SS;. Biochemistry 1995;34:8406-8414. (from Pfam)

Date:

2024-10-16

This entry contains many divergent copper oxidase-like domains that are not recognised by the Pfam:PF00394 model. [1]. 2404764. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Messerschmidt A, Huber R;. Eur J Biochem 1990;187:341-352. [2]. 1548698. Refined crystal structure of ascorbate oxidase at 1.9 A resolution. Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano L, Petruzzelli R, Rossi A, Finazzi-Agro A;. J Mol Biol 1992;224:179-205. [3]. 10573417. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Page CC, Moser CC, Chen X, Dutton PL;. Nature 1999;402:47-52. [4]. 7599131. X-ray absorption studies and homology modeling define the structural features that specify the nature of the copper site in rusticyanin. Grossmann JG, Ingledew WJ, Harvey I, Strange RW, Hasnain SS;. Biochemistry 1995;34:8406-8414. (from Pfam)

Date:

2024-10-16

Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain. [1]. 2404764. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Messerschmidt A, Huber R;. Eur J Biochem 1990;187:341-352. [2]. 1548698. Refined crystal structure of ascorbate oxidase at 1.9 A resolution. Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano L, Petruzzelli R, Rossi A, Finazzi-Agro A;. J Mol Biol 1992;224:179-205. (from Pfam)

Date:

2024-10-16

Many proteins that fold in the cytosol because a required cofactor is available there only, or because cytosolic chaperones assist in folding, or because high salt in the extracellular milieu would interfere with folding there, cannot rely on the standard general secretory (Sec) pathway for secretion across the plasma membrane. This model describes a family of predicted long, non-Sec signal sequences and signal-anchor sequences (uncleaved signal sequences). All contain a typically invariant pair of arginine residues, in a motif approximated by (S/T)-R-R-X-F-L-K, followed by a membrane-spanning hydrophobic region. The system that secretes pre-folded proteins with this motif is known as twin-arginine translocation, or TAT. Note that some variant forms, often lineage-specific ones such as the RKxFL version found in Leptospira, do occur but typically fall outside the scope of this HMM. Twin-arginine signal domains with small amino acid side chains at the -1 and -3 positions from the C-terminus of the model should be predicted to be cleaved as are Sec pathway signal sequences. The system, although far from universal in prokaryotes, is widespread in bacteria and present also in many archaea.

Date:

2019-11-27

This HMM represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export.

Date:

2024-06-21

PcoA, a multicopper oxidase related to laccase and bilirubin oxidase, belongs to a mobile system for copper resistance. It catalyzes oxidation of the more toxic Cu(+), or Cu(I), to the less toxic Cu2+), or Cu(II).

Gene:

pcoA

Date:

2018-01-16