Protein Family Models

Iteration of the HHE family ([2]) found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain ([1]) in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor Swiss:P80255 binds Cadmium so as to protect the organism from toxicity ([3]). However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial Swiss:Q7WX96 is a regulator of response to NO, which suggests yet another set-up for its metal ligands ([4]). In Staphylococcus aureus P72360 has been noted to be important when the organism switches to living in environments with low oxygen concentrations ([4]); perhaps this protein acts as an oxygen store or scavenger. This domain can bind oxygen (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043) [1]. 678527. Structure of methemerythrin at 2.8-Angstrom resolution: computer. graphics fit of an averaged electron density map.. Stenkamp RE, Sieker LC, Jensen LH, McQueen JE Jr;. Biochemistry 1978;17:2499-2504.. [2]. 12625841. New Knowledge from Old: In silico discovery of novel protein. domains in Streptomyces coelicolor.. Yeats C, Bentley S, Bateman A;. BMC Microbiol 2003;3:3-3.. [3]. 9188702. Structures of wild-type chloromet and L103N hydroxomet Themiste. zostericola myohemerythrins at 1.8 A resolution.. Martins LJ, Hill CP, Ellis WR Jr;. Biochemistry 1997;36:7044-7049.. [4]. 11513618. The srhSR gene pair from Staphylococcus aureus: genomic and. proteomic approach. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

bacteriohemerythrin is an oxygen-binding protein that may be involved in a storage mechanism or for delivery to oxygen-requiring enzymes

Date:

2019-10-11

This model describes both members of the hemerythrin (TIGR00058) family of marine invertebrates and a broader collection of bacterial and archaeal homologs. Many of the latter group are multidomain proteins with signal-transducing domains such as the GGDEF diguanylate cyclase domain (TIGR00254, PF00990) and methyl-accepting chemotaxis protein signaling domain (PF00015). Most hemerythrins are oxygen-carriers with a bound non-heme iron, but at least one example is a cadmium-binding protein, apparently with a role in sequestering toxic metals rather than in binding oxygen. Patterns of conserved residues suggest that all prokaryotic instances of this domain bind iron or another heavy metal, but the exact function is unknown. Not surprisingly, the prokaryote with the most instances of this domain is Magnetococcus sp. MC-1, a magnetotactic bacterium.

Date:

2024-05-30

Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is named based on its homology to eukaryotic proteins such as myohemerythrin.

Date:

2021-06-28