Cfrench:multidomhem
Analysis of multi-domain proteins with putative hemerythrin-like domains
Our analysis showed a variety of large multi-domain proteins with a hemerythrin-like domain, usually at the C-terminus or N-terminus. Other domains present were generally identified by sequence comparison as being involved in signalling: mainly methyl-accepting chemotaxis proteins (MCPs), diguanylate cyclases (GGDEF domains), histidine kinase domains, CheY-like response receiver domains, and cAMP-binding domains, and in one case an apparent phosphatase domain. The most obvious interpretation is that the hemerythrin domains act as oxygen sensors, and the auxiliary domains function in signal transduction to alter the cell's state. Sequence comparisons allowed the majority of the putative multi-domain hemerythrins to be assigned to a few well defined families.
MCP-hemerythrins
These proteins contain a large N-terminal MCP-like region and a C-terminal hemerythrin-like region. The most obvious interpretation is that they function in aerotaxis. Sequence analysis shows that they fall into three groups.
Magnetospirillum/Rhodospirillum MCP-hemerythrinsMagms807 | Magnetospirillum magnetotacticum MS1 | Magn03010970 |
Magms699 | Magnetospirillum magnetotacticum MS1 | Magn03011185 |
Magam807 | Magnetospirillum magneticum AMB1 | amb0220 |
Magam665 | Magnetospirillum magneticum AMB1 | amb3267 |
Magam810 | Magnetospirillum magneticum AMB1 | amb3793 |
Magam795 | Magnetospirillum magneticum AMB1 | amb4156 |
Rhoru736 | Rhodospirillum rubrum ATCC 11170 | Rru_A0632 |
Sequence comparisons show that Magms807 and Magma807 are specific homologs, as are Magms699 and Magam810. Rhoru736 is least closely related to the others.