The domain within your query sequence starts at position 522 and ends at position 667; the E-value for the GCV_T domain shown below is 1.4e-29.

VIDMSSFTKFEITSTGDEALESLQYLFCNDLDVPVGHIVHTGMLNEYGGYENDCSIARLT
KRSFFMISPTDQQVHCWAWLNKYLPKDSNLLLEDVTWKYTALNLIGPRAVDVLSELSYAP
MTPDHFPTLFCKSPPEKTLGWSSLFL

GCV_T

GCV_T
PFAM accession number:PF01571
Interpro abstract (IPR006222):

This domain is found at the N terminus of glycine cleavage T-proteins, which are part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyses the catabolism of glycine in eukaryotes. The T-protein (aminomethyltransferase, EC 2.1.2.10) is a folate-dependent enzyme that catalyses the release of ammonia and the transfer of the methylene carbon unit (C1 unit) to tetrahydrofolate (H4folate) from the aminomethyl intermediate attached to the lipoate cofactor of H-protein [(PUBMED:9047339), (PUBMED:16051266)].

This domain is also found in YgfZ proteins. YgfZ in E.coli is a folate binding protein involved in RNA modification and regulation of chromosomal replication initiation [(PUBMED:16359333)]. YgfZ is not an aminomethyltransferase but is likely a folate-dependent regulatory protein [(PUBMED:15489424)]. This domain could represent a folate-binding domain.

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