The domain within your query sequence starts at position 10 and ends at position 105; the E-value for the Acylphosphatase domain shown below is 1.5e-26.

MTELLKSVDYEVFGTVQGVCFRMYTEGEAKKRGLVGWVKNTSKGTVTGQVQGPEEKVDAM
KSWLSKVGSPSSRIDRADFSNEKTISKLEYSDFSIR

Acylphosphatase

Acylphosphatase
PFAM accession number:PF00708
Interpro abstract (IPR001792):

Acylphosphatase (EC 3.6.1.7) is an enzyme of approximately 98 amino acid residues that specifically catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates [(PUBMED:1664426)], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate [(PUBMED:2538623)]. The enzyme has a mainly beta-sheet structure with 2 short alpha-helical segments. It is distributed in a tissue-specific manner in a wide variety of species, although its physiological role is as yet unknown [(PUBMED:2538623)]: it may, however, play a part in the regulation of the glycolytic pathway and pyrimidine biosynthesis [(PUBMED:2830253)]. There are two known isozymes. One seems to be specific to muscular tissues, the other, called 'organ-common type', is found in many different tissues. A number of bacterial and archebacterial hypothetical proteins are highly similar to that enzyme and that probably possess the same activity.

An acylphosphatase-like domain is also found in some prokaryotic hydrogenase maturation HypF carbamoyltransferases [(PUBMED:9799289), (PUBMED:12206761)].

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