SMART: Pfam domain AMP-binding

The domain within your query sequence starts at position 147 and ends at position 501; the E-value for the AMP-binding domain shown below is 5.3e-50.

DPCCTASAAAVRVRSCWPQLGLPTLVEFLESLEPDLPALRAMGLHLWATGPETNVAGISN
LLSEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCG
VHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIG
ELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFN
YTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQS
PFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWK

AMP-binding

PFAM accession number:	PF00501
Interpro abstract (IPR000873):	A number of prokaryotic and eukaryotic enzymes, which appear to act via an ATP-dependent covalent binding of AMP to their substrate, share a region of sequence similarity [ (PUBMED:2118102) (PUBMED:2911486) (PUBMED:2254270) ]. This region is a Ser/Thr/Gly-rich domain that is further characterised by a conserved Pro-Lys-Gly triplet. The family of enzymes includes luciferase, long chain fatty acid Co-A ligase, acetyl-CoA synthetase and various other closely-related synthetases [ (PUBMED:26473393) ].

PFAM accession number:

PF00501

Interpro abstract (IPR000873):

A number of prokaryotic and eukaryotic enzymes, which appear to act via an ATP-dependent covalent binding of AMP to their substrate, share a region of sequence similarity [ (PUBMED:2118102) (PUBMED:2911486) (PUBMED:2254270) ]. This region is a Ser/Thr/Gly-rich domain that is further characterised by a conserved Pro-Lys-Gly triplet. The family of enzymes includes luciferase, long chain fatty acid Co-A ligase, acetyl-CoA synthetase and various other closely-related synthetases [ (PUBMED:26473393) ].

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