ID   E2BE73_HARSA            Unreviewed;       607 AA.
AC   E2BE73;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
GN   ORFNames=EAI_10685 {ECO:0000313|EMBL:EFN86010.1};
OS   Harpegnathos saltator (Jerdon's jumping ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX   NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN   [1] {ECO:0000313|EMBL:EFN86010.1, ECO:0000313|Proteomes:UP000008237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN86010.1,
RC   ECO:0000313|Proteomes:UP000008237};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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   EMBL; GL447756; EFN86010.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2BE73; -.
DR   STRING; 610380.E2BE73; -.
DR   EnsemblMetazoa; XM_011138853.3; XP_011137155.1; LOC105181836.
DR   InParanoid; E2BE73; -.
DR   OMA; CNPAMGG; -.
DR   Proteomes; UP000008237; Unassembled WGS sequence.
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   Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008237}.
FT   DOMAIN          522..594
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
SQ   SEQUENCE   607 AA;  68248 MW;  13F0A59A64F8F2A0 CRC64;
     MGAKTLLVTQ KKSTIGEMSC NPSFGGIGKG HLMREVDALD GVCCRICDIS GIHYKILNKR
     KGPAVWGLRA QIDRKLYKKH LQAELFNMPG LHICESSVED LILANDSLSC RGVILKDGTK
     IFGDSVVITT GTFLKGQINI GLEKRPAGRM DDEPSIGLAN TLDRLGFRVG RLKTGTPPRL
     EKESIDFTKC IKHLPDECPI PFSFMNNKVW LLPDEQVPTY LTYTNKNVAK IIRDNMHCNL
     HVTEEITGPR YCPSIESKVL RFATTTHQVW LELEGLDSPL IYPSGLSCTL PEEKQVELVK
     CILGLENARL ARPGYGVEYD YIDPRELTSE LETKKIPGLF LAGQINGTTG YEEAAAQGII
     AGVNAAAKVL KKPPLVISRT EGYIGVLIDD LTTQGTTEPY RMFTSRAEFR LSLRPDNADH
     RLTEKGYKVG CVSRERMDRT WNTQRKIQEA IQLLQSERQS NHKWRHMLKL KHTKSIQNKS
     AFDILGNTND EITFAQLAKI LPELLGHLDG DPTLMIRVEI EAKYAFVVAN QQNQVDDIRR
     NEQMIIPEDI DYNSNELNLS NEDKEKLTKY LPRTIAAANK ISGVTPIAIL KLLYYIRHRS
     SEYIAKV
//