The domain within your query sequence starts at position 109 and ends at position 366; the E-value for the TauD domain shown below is 6.9e-48.

FLPECQYWGSELQLPTLNFEDVLNDDDHAYKWLSSLKKVGIVRLTGAADKRGEIIKLGKR
IGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGD
SEIVDGFNVCQKLKEKNPQAFHILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVR
VNFNNATRDTVFDVPIERVQPFYAALKEFVDLMNSKEYKYTFKMNPGDVITFDNWRLLHG
RRSYEAGTEISRHLEGAY

TauD

 TauD
PFAM accession number:PF02668
Interpro abstract (IPR003819):

This domain is found in TauD/TfdA taurine catabolism dioxygenases. The Escherichia coli tauD gene is required for the utilisation of taurine (2-aminoethanesulphonic acid) as a sulphur source and is expressed only under conditions of sulphate starvation. TauD is an alpha-ketoglutarate-dependent dioxygenase catalysing the oxygenolytic release of sulphite from taurine [ (PUBMED:9287300) ]. The 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. (strain RASC) also belongs to this family [ (PUBMED:8779585) ]. TfdA from Ralstonia eutropha (Alcaligenes eutrophus) is a 2,4-D monooxygenase [ (PUBMED:3036764) ].

This domain is also found in gamma-butyrobetaine hydroxylase (GBBH), the enzyme responsible for the biosynthesis of L-carnitine, a key molecule of fatty acid metabolism. The GBBH monomer consists of this catalytic double-stranded beta-helix (DBSH) domain, which is found in all 2-ketoglutarate (2KG) oxygenases, and a smaller N-terminal domain [ (PUBMED:20599753) ].

GO process:oxidation-reduction process (GO:0055114)
GO function:oxidoreductase activity (GO:0016491)

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