Protein Family Models

This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface [1]. [1]. 9036855. Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Boyington JC, Gladyshev VN, Khangulov SV, Stadtman TC, Sun PD;. Science. 1997;275:1305-1308. (from Pfam)

Date:

2024-10-16

This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyses the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor [1]. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules [2]. [1]. 9818358. The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme. Hochheimer A, Hedderich R, Thauer RK;. Arch Microbiol 1998;170:389-393. [2]. 8890912. Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution. Schneider F, Lowe J, Huber R, Schindelin H, Kisker C, Knablein J;. J Mol Biol 1996;263:53-69. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Gene:

dmsA

Date:

2023-07-22

anaerobic dimethyl sulfoxide reductase subunit A is the catalytic component of the enzyme that catalyzes the reduction of dimethylsulfoxide to dimethylsulfide

Date:

2017-02-03

Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The putative selenate reductase system paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.

Date:

2024-05-30

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