ID   A0A0R3RUB7_9BILA        Unreviewed;       628 AA.
AC   A0A0R3RUB7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000561301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000561301-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; A0A0R3RUB7; -.
DR   STRING; 1147741.A0A0R3RUB7; -.
DR   WBParaSite; EEL_0000561301-mRNA-1; EEL_0000561301-mRNA-1; EEL_0000561301.
DR   Proteomes; UP000050640; Unplaced.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR049312; GIDA_C_N.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR047001; MnmG_C_subdom.
DR   InterPro; IPR044920; MnmG_C_subdom_sf.
DR   InterPro; IPR040131; MnmG_N.
DR   NCBIfam; TIGR00136; gidA; 1.
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; PF13932; GIDA_C; 1.
DR   Pfam; PF21680; GIDA_C_1st; 1.
DR   SMART; SM01228; GIDA_assoc_3; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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          552..623
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
SQ   SEQUENCE   628 AA;  70352 MW;  2DB418274CD9A950 CRC64;
     MLRKTLSTLT AGNEPVIYDV IVIGGGHAGC EAATAAARCS ARTLLLTNRK DTIGEMSCNP
     SFGGVGKGHL IREVDALDGL CGRICDKSAI NYHALNSSHG PAVLGLRAQI DRKLYKEHMQ
     HEILNCTKGL DVMEKAVDDL IIKRKYGEIP RVVGVVADDQ ILKAKALVVT TGTFLGGKLF
     RGSESYAAGR LGEKASSKLS ETFKRLGFKL GRFRTGTPAR LLKKTIDFSK FSPQYPDRKP
     IPFSFLTEHI WLPYHQQLPS YLGFTNSRLA EVILKHFNDC NYIRSEANGP RYCPSLESKI
     FLEHEGLDSD LIYPQGMSMT FSPEVQLEVY RCIPGLEDVE ISEAGYGVEY DYVDPKQLKS
     TLQPKTVEGL FLAGQINGTT GYEEAAAQGI VAGINAAASS QNKEPFVIDR TEGYIGVLID
     DLTSLGTSEP YRMFTSRAEL RLHLRPDNAD MRLTKKGYQH GAVSEYRYNR FLKILSAYNE
     AQDLLKSVKY PMNFWKKFMP HMGNGQKPKV YSAFDLLCRY ETDFMAFRKA APVELEGLPK
     NEEIENRLKI EAFYHFYLEK SLAKIERIRE ECATLIPEDF DYSKMKSVST ECKENFEFWR
     PQNLAAASRV PGATTDALME LLSFLKAP
//