The domain within your query sequence starts at position 521 and ends at position 697; the E-value for the Flavodoxin_1 domain shown below is 4.8e-54.

ILYGSETGRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHEALVLVVTSTFGNGDPPE
NGESFAAALMEMSGPYNSSPRPEQHKSYKIRFNSVSCSDPLVSSWRRKRKESSNTDSAGA
LGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGW

Flavodoxin_1

Flavodoxin_1
PFAM accession number:PF00258
Interpro abstract (IPR008254):

The flavodoxin-like domain is an around 170-residue domain with a flavin mononucleotide (FMN)-binding site. It is involved in electron transfer reactions [(PUBMED:8160268), (PUBMED:7756978)].

Structure analyses of several flavodoxin-like domains have shown that it is a wound alpha-beta-alpha fold with a central 5-stranded parallel hydrophobic beta-sheet flanked on either side by amphipathic alpha-helices [(PUBMED:9237990), (PUBMED:10048323), (PUBMED:10610791)]. The FMN is positioned at the tip of the C-terminal side of the beta-sheet [(PUBMED:9237990)]. The fold correlates with a highly conserved, repetitive sequence pattern in which hydrophobic residues cluster in beta-strands and have a 3-4-residue periodicity in alpha-helices [(PUBMED:7756978)].

This domain is found in a number of proteins including flavodoxin and nitric-oxide synthase. Flavodoxins are electron-transfer proteins that function in various electron transport systems. They bind one FMN molecule, which serves as a redox-active prosthetic group [(PUBMED:2597140)] and are functionally interchangeable with ferredoxins. They have been isolated from prokaryotes, cyanobacteria, and some eukaryotic algae. Nitric oxide synthase (EC 1.14.13.39) produces nitric oxide from L-arginie and NADPH. Nitric oxide acts as a messenger molecule in the body.

GO function:FMN binding (GO:0010181)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Flavodoxin_1