ID   A0A0N5AT89_9BILA        Unreviewed;       639 AA.
AC   A0A0N5AT89;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000803401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000803401-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; A0A0N5AT89; -.
DR   STRING; 451379.A0A0N5AT89; -.
DR   WBParaSite; SMUV_0000803401-mRNA-1; SMUV_0000803401-mRNA-1; SMUV_0000803401.
DR   Proteomes; UP000046393; 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; 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          559..629
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
SQ   SEQUENCE   639 AA;  70805 MW;  3A937E51F9AB78B0 CRC64;
     MAGALSRVAN SLVYDVVVVG GGHAGCEAAA AASRVGARTV LITHQVEKIG EMSCSPSFGG
     IGKGHLIREV DAMDGVCARI CDKSAINYRV LNAGAGPAVY GLRAQIDRAL YKEHMKKEIL
     SNTPNLTVIE GTIDDLSVCT NYQNKLSVNG VVMNNGQVIT AKSVVITSGT FLGGVIFQGM
     NKQYGGRVGE KSAICLSRSL KKLGFKTARL RTGTPPRLLK SSIDFNKFTP IYPDEKPILF
     SFLSKRCWLS PSKQIPSFLT FTNQKVAEIV RENYRKSEYI RSDSNGPRYC PSLEAKILKF
     GSLNHRVFLE IEGLNSNLVY PQGMSMTFGT DVQLEVLRAI PGLEKVEIVR PGYGVEYDFV
     DPKQLNPSLE TKIIQGLFLA GQINGTTGYE EAAAQGILAG INAGIISCGK QLYIDRTEAY
     IGVLVDDLTS LGTSEPYRMF TSRAEFRLFL RPDNADLRLT EKANLVGAIS AERYKHFCKT
     RSNFLTVAKI LQDIKYSLTK WTSLIPSIVA AKDSGKVLSA YDMLYRYHVS LHDIERIFPN
     SLLPYLDDDT LEFRIRTHAL YEAQHKQLVN KMEEVKRECK IQIPENIDYQ KMNLSLECRE
     KLEEWRPQNL AAASRIPGVT PEALIQIWRS VKSGTVPVA
//