The domain within your query sequence starts at position 967 and ends at position 1236; the E-value for the ABC_membrane domain shown below is 8.6e-48.

TLSICLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNKTSVRLGVYAALGILQGLLVMLSA
FTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILML
LNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSH
FSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFA
ALFAVIGRNSLNPGLVGLSVSYALQVTMAL

ABC_membrane

ABC_membrane
PFAM accession number:PF00664
Interpro abstract (IPR011527):

This entry represents the transmembrane domain in cases where the TMD and ABC region are found in the same protein.

ABC transporters minimally contain two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). In certain bacterial transporters, these regions are found on different polypeptides. The function of the integral inner-membrane protein is to translocate the substrate across the membrane, as well as in substrate recognition [ (PUBMED:9873074) (PUBMED:10529352) ].

ABC transporters belong to the ATP-Binding Cassette (ABC) superfamily, which uses the hydrolysis of ATP to energise diverse biological systems. ABC transporters minimally consist of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These can be found on the same protein or on two different ones. Most ABC transporters function as a dimer and therefore are constituted of four domains, two ABC modules and two TMDs.

ABC transporters are involved in the export or import of a wide variety of substrates ranging from small ions to macromolecules. The major function of ABC import systems is to provide essential nutrients to bacteria. They are found only in prokaryotes and their four constitutive domains are usually encoded by independent polypeptides (two ABC proteins and two TMD proteins). Prokaryotic importers require additional extracytoplasmic binding proteins (one or more per systems) for function. In contrast, export systems are involved in the extrusion of noxious substances, the export of extracellular toxins and the targeting of membrane components. They are found in all living organisms and in general the TMD is fused to the ABC module in a variety of combinations. Some eukaryotic exporters encode the four domains on the same polypeptide chain [ (PUBMED:9873074) ].

The ATP-Binding Cassette (ABC) superfamily forms one of the largest of all protein families with a diversity of physiological functions [ (PUBMED:9873074) ]. Several studies have shown that there is a correlation between the functional characterisation and the phylogenetic classification of the ABC cassette [ (PUBMED:9873074) (PUBMED:11421270) ]. More than 50 subfamilies have been described based on a phylogenetic and functional classification [ (PUBMED:9873074) (PUBMED:11421269) (PUBMED:11421270) ]; (for further information see http://www.tcdb.org/tcdb/index.php?tc=3.A.1).

GO process:transmembrane transport (GO:0055085)
GO component:integral component of membrane (GO:0016021)
GO function:ATPase-coupled transmembrane transporter activity (GO:0042626), ATP binding (GO:0005524)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ABC_membrane