ID   A0A183H4W0_9BILA        Unreviewed;       409 AA.
AC   A0A183H4W0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
GN   ORFNames=OFLC_LOCUS2522 {ECO:0000313|EMBL:VDO33268.1};
OS   Onchocerca flexuosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0000251901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:OFLC_0000251901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO33268.1, ECO:0000313|Proteomes:UP000267606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; UZAJ01001466; VDO33268.1; -; Genomic_DNA.
DR   STRING; 387005.A0A183H4W0; -.
DR   WBParaSite; OFLC_0000251901-mRNA-1; OFLC_0000251901-mRNA-1; OFLC_0000251901.
DR   Proteomes; UP000050787; Unplaced.
DR   Proteomes; UP000267606; Unassembled WGS sequence.
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; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          19..400
FT                   /note="MnmG N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01134"
SQ   SEQUENCE   409 AA;  45292 MW;  BE5A983BED48BC44 CRC64;
     MLRRTLSTLI PRNEAVKYDV IVIGGGHAGC EAAAAAARCC VSTLMLTSKK DTIGEMSCNP
     SFGGVGKGHL IREVDALDGL CGRICDKSAI NYHALNASHG PAVLGLRAQI DRKLYKEYMQ
     HEILSCTEGL DVMEKTVDDL IIEYKEGEVP QVVGVVADGQ ILKAKAVVVT TGTFLGGKLF
     RGSESYAAGR LGEKASSKLS ETFKRLGFKL GRFRTGTPAR LLKKTIDFNK FTPQYPDLKP
     IPFSFLTEHI WIPYRQQLPS YLGYTNNRLA EVVLKHFNEC SYIRSEANGP RYCPSLESKV
     IRFPHLNHRV FLEHEGLDSD LIYPQGMSMT FAPEVQLEVY RCIPGLENVE LSEAGYGVEY
     DYVDPKQLKP TLQTKLVDSL FFAGQINGTT GYEEAAAQGS FVNFFSFDI
//