ID   A0A0R3QA36_9BILA        Unreviewed;       322 AA.
AC   A0A0R3QA36;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
OS   Brugia timori.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0000320201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BTMF_0000320201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Involved in the 5-carboxymethylaminomethyl modification
CC       (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
CC       {ECO:0000256|ARBA:ARBA00002739}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the MnmG family.
CC       {ECO:0000256|ARBA:ARBA00007653}.
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DR   AlphaFoldDB; A0A0R3QA36; -.
DR   STRING; 42155.A0A0R3QA36; -.
DR   WBParaSite; BTMF_0000320201-mRNA-1; BTMF_0000320201-mRNA-1; BTMF_0000320201.
DR   Proteomes; UP000050602; Unplaced.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR049312; GIDA_C_N.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR040131; MnmG_N.
DR   PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR   PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF21680; GIDA_C_1st; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          4..157
FT                   /note="MnmG N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01134"
FT   DOMAIN          218..313
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal N-terninal subdomain"
FT                   /evidence="ECO:0000259|Pfam:PF21680"
SQ   SEQUENCE   322 AA;  36941 MW;  68E511C81D9B90E1 CRC64;
     LPSYLGFTNN LLAQMVLKHF NECNYIRSEA NGPRYCPSLE SKVIRFPHLN HRIFLEPEGL
     DSDLIYPQGM SMTFAPEVQL EVYRCIPGLE NVEISQAGYG IEYDYVDPKQ LKLTLQTKAV
     EGLFLAGQIN GTTGYEEAAA QGIVAGINAA ASSQNKKPFV IDRTEGYIGV LIDDLTSLGT
     SEPYRMFTSR AELRLHLRPD NADMRLTKKG YEHGAVSEHR YNRFLKMLSA YNKAQDLLKS
     IKYPMNFWKK LLPCLENARV TKVYSAFDLL CRYEVDFMEI QKAVPFELER LLENKEIEYR
     LKIEAFYYFY LDKSLAKVST II
//