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Database: UniProt
Entry: A0A1A9WNB1_9MUSC
LinkDB: A0A1A9WNB1_9MUSC
Original site: A0A1A9WNB1_9MUSC 
ID   A0A1A9WNB1_9MUSC        Unreviewed;       665 AA.
AC   A0A1A9WNB1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
OS   Glossina brevipalpis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI025923-PA, ECO:0000313|Proteomes:UP000091820};
RN   [1] {ECO:0000313|Proteomes:UP000091820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GBRI025923-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI025923-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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; A0A1A9WNB1; -.
DR   STRING; 37001.A0A1A9WNB1; -.
DR   EnsemblMetazoa; GBRI025923-RA; GBRI025923-PA; GBRI025923.
DR   VEuPathDB; VectorBase:GBRI025923; -.
DR   OrthoDB; 5486689at2759; -.
DR   Proteomes; UP000091820; 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   HAMAP; MF_00129; 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}.
FT   DOMAIN          578..650
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
SQ   SEQUENCE   665 AA;  74897 MW;  2C98DCC11FBD661C CRC64;
     MFRFYSKNFK NVITTVVRFN SFARNTSLEY DVLVIGGGHA GTEACAAAAR MGARTLLVTH
     KRETIGEMSC NPSFGGIGKG HLVREVDAMD GVCAKCCDKS GVQYKILNRR RGPAVWGPRA
     QIDRILYKKA IQEYIFNMEN LDILSAPVDN LLIEPTAEGE SMQCKGIILQ NGQILKSRTV
     VLTTGTFLRA NINFGLEVRP AGRMGDAPAM ALGKNLEDLG FRMGRLKTGT PPRLLRNTID
     FSQLSKNIGD NPPVPFSFMN DCVWIQADAQ LPCYLTYTTM KVNQIVKDNL HVNRHVTEEI
     TGPRYCPSIE SKVLRFGEKS HQIWLEPEGF ESDVIYPQGL SCTLPYEQQE ELVHSIPGLQ
     KAQIKQPGYG VEYDYIDPRE LFSTLETKRV QNLFFAGQIN GTTGYEEAAA QGIIAGANAA
     AKTVHKDVKN LTISRTEGYI GVLIDDLTTL GTNEPYRMFT SRSEFRLMLR PDNADLRLTE
     KAFNFGLVRK ERYERYLAIR NQLSEAADLL KSIKKRTNDW RQSLHLPTAK VSVEKSAFDM
     LGIPSDNITL KQLIDLLPQE LGHLNNVKAL EDRIKIQALY SYFIEEQMHQ VNEVRREENL
     IIPRDIDYFS KSLSLSNEER QKLTMIQPQT IAAASRIQGV TPSTVVRLLK FVKRIDQANI
     MLCNP
//
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