The domain within your query sequence starts at position 1 and ends at position 171; the E-value for the Proton_antipo_M domain shown below is 2.9e-47.
AIEGPTPVSALLHSSTIVVAGIFLLVRFHPLTTNNNFILTTILCLGALTTLFTAICALTQ NDIKKIVAFSTSNQLGLIIVTLGINQPYLAFLHICTHAFFKAILFICSGSIIHSLADEQD IRKIGNITKTIPFTSSCLVIGSLALTGMPFLTGFYSKDLIIEAINTCNTNT
Proton_antipo_M |
---|
PFAM accession number: | PF00361 |
---|---|
Interpro abstract (IPR001750): | Mrp-type antiporters comprise the cation/proton antiporter family 3 (CPA3), commonly referred to as Mrp. They are the products of operons that carry either six or seven genes (mrpA-G), and form complexes containing all subunits [ (PUBMED:15980940) (PUBMED:18408029) ]. They have Na(+)/H(+) antiporter activity [ (PUBMED:24142251) ]. Two of the Mrp proteins, MrpA and MrpD, resemble NuoL/ND5, NuoM/ND4, NuoN/ND2, the homologous subunits that constitute the membrane-embedded, proton-translocating core of complex I [ (PUBMED:12914915) (PUBMED:20826797) (PUBMED:12460669) (PUBMED:20595580) ]. They also resemble subunits of membrane-bound hydrogenases, such as HyfB, HyfD and HyfF from E.coli [ (PUBMED:9387241) ] and F420H2 dehydrogenasa (FPO complex) subunits L, N and M [ (PUBMED:10751389) ]. This domain is found in subunits NuoL/ND5, NuoM/ND4, and NuoN/ND2 of the NADH:quinone oxidoreductase (complex I), Mrp antiporters subunits A and D, and in membrane subunits of hydrogenase complexes, such as hydrogenase-4 and F420H2 dehydrogenase. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Proton_antipo_M