The domain within your query sequence starts at position 1029 and ends at position 1304; the E-value for the Hydrolase domain shown below is 1.3e-40.

VKVVVFDKTGTITHGTPVVNQVKVLVESNKISRNKILAIVGTAESNSEHPLGAAVTKYCK
KELDTETLGTCTDFQVVPGCGISCKVTNIEGLLHKSNLKIEENNIKNASLVQIDAINEQS
STSSSMIIDAHLSNAVNTQQYKVLIGNREWMIRNGLVISNDVDESMIEHERRGRTAVLVT
IDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEV
LPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMAN

Hydrolase

Hydrolase
PFAM accession number:PF00702
Interpro abstract (IPR023214):

The haloacid dehydrogenase (HAD) superfamily includes phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, which are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification[(PUBMED:7966317)].

Crystal structures of proteins from the HAD superfamily show that these proteins all share a conserved alpha/beta-domain classified as a hydrolase fold, which is similar to the Rossmann fold [(PUBMED:14555659)]. This conserved domain usually contains an insertion (sub)domain. For example, the crystal structure of a phosphoglycolate phosphatase from Thermoplasma acidophilum [(PUBMED:14555659)] revealed two distinct domains, a larger core domain and a smaller cap domain. The large domain is composed of a centrally located five-stranded parallel beta-sheet with strand order S10, S9, S8, S1, S2 and a small beta-hairpin, strands S3 andS4. This central sheet is flanked by a set of three aplha-helices on one side and two helices on the other. The topology of the large domain is conserved; however, structural variation is observed in the smaller domain among the different functional classes of the haloacid dehalogenase superfamily.

This entry represents the large domain with conserved topology among the HAD superfamily.

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