The domain within your query sequence starts at position 73 and ends at position 490; the E-value for the ADP_PFK_GK domain shown below is 1.9e-140.

RRVAVGVNACVDVVISGVKLLQALGLSPGSGKDHAILHSRSDLEEAFLYFMGKGAAAERF
FSDKETFHDIAQAASEFPGAQHYVGGNAALIGQRFAANTDLKVLLCGPIGPKLHELLDDN
VFVPPESLQEEDEFHLILEYLAGEEWGPFKAPHANRFIFSHDLSNGAMNMLEVFVSSLEE
FQPDLVVLSGLHMMEGQSKELQRKRLLEVVTAISDIPTGIPVHLELASMTNRELMSSIVH
QVFPTVASLGLNEQELLFLSQSASGPHASLSSWDGVPDVGMVSDILFWILKEHGRSENRA
SDLTRIHFHTLVYHILATVDGHWANQLAAVAAGARVAGTQACATETIDTNRVSLRAPQEF
TTSHLESGSRIVLNPDKPVVEWHREGITFHFTPVLVCKDPVRTVGLGDAISAEGLFYS

ADP_PFK_GK

 ADP_PFK_GK
PFAM accession number:PF04587
Interpro abstract (IPR007666):

Although ATP is the most common phosphoryl group donor for kinases, certain hyperthermophilic archaea, such as Thermococcus litoralis and Pyrococcus furiosus, utilise unusual ADP-dependent glucokinases (ADPGKs) and phosphofructokinases (ADPPKKs) in their glycolytic pathways [ (PUBMED:11286887) (PUBMED:12237466) (PUBMED:12909015) ]. ADPGKs and ADPPFKs exhibit significant similarity, and form an ADP-dependent kinase (ADPK) family, which was tentatively named the PFKC family [ (PUBMED:11778837) ]. A ~460-residue ADPK domain is also found in a bifunctional ADP-dependent gluco/phosphofructo- kinase (ADP-GK/PFK) from Methanocaldococcus jannaschii (Methanococcus jannaschii) as well as in homologous hypothetical proteins present in several eukaryotes [ (PUBMED:11717273) ].

The whole structure of the ADPK domain can be divided into large and small alpha/beta subdomains. The larger subdomain, which carries the ADP binding site, consists of a twisted 12-stranded beta sheet flanked on both faces by 13 alpha helices and three 3(10) helices, forming an alpha/beta 3-layer sandwich. The smaller subdomain, which covers the active site, forms an alpha/beta two-layer structure containing 5 beta strands and four alpha helices. The ADP molecule is buried in a shallow pocket in the large subdomain. The binding of substrate sugar induces a structural change, the small domain closing to form a complete substrate sugar binding site [ (PUBMED:11286887) (PUBMED:12237466) (PUBMED:12909015) ].

GO process:carbohydrate metabolic process (GO:0005975)
GO function:phosphotransferase activity, alcohol group as acceptor (GO:0016773)

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