ID A0A0L0BSJ7_LUCCU Unreviewed; 667 AA.
AC A0A0L0BSJ7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
GN ORFNames=FF38_12155 {ECO:0000313|EMBL:KNC23017.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC23017.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC23017.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC23017.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC23017.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC23017.1}.
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; JRES01001422; KNC23017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0BSJ7; -.
DR STRING; 7375.A0A0L0BSJ7; -.
DR EnsemblMetazoa; KNC23017; KNC23017; FF38_12155.
DR OMA; CNPAMGG; -.
DR Proteomes; UP000037069; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069}.
FT DOMAIN 583..655
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 667 AA; 74789 MW; 2FF07A13C151F1F4 CRC64;
MLLFQKAYIK CFAQKRLLSY AQRNKDSKVF DVVVIGGGHA GTEACAAAAR MGARTLLVTH
KIDTIGEMSC NPSFGGIGKG HLMREIDALG GLCGRMCDKS GVQYKVLNKR RGPAVWGPRA
QIDRKLYKKA VQNEIFGMKN LEILSASVDD LFIEADRENE NKAKCKGIVL DSGQIIHSST
VVLTTGTFLR ANINFGLEVK PAGRMGDAPA IALGKSIENL GFSMGRLKTG TPPRISKESI
DYNKLEAHYG DNPPLPFSYM NEKVWINADE QLPCHLTYTS LKVNKIVKEN MHLNRHVTEE
INGPRYCPSI ESKVLRFGEK QHQIWLEPEG FDSDLIYPQG LSCTLPYEQQ VELVNSIYGL
EKAKVVQPGY GVEYDYIDPR ELYPSLETKR VNNLYFAGQL NGTTGYEEAA AQGIIAGANA
AAKSKQFGER EITRQLTISR TEGYIGVLID DLTSLGTNEP YRMFTSRAEF RLSLRPDNAD
LRLTEKGYNF GLVSEDQYKH FIKIKNYLDE TKALLTSIKK HSNYWREHIG LAKSKSSVEK
TAFEMLGIPS DNITLQHLVK IIPDELGKIQ QVESIAERIK IEALYAHFVE EQLKDAEQVR
KEECLIIPKD IDYFSKSLSL SNEERQKLTM MQPQTIAAAS RIQGVTPATI VRLLKHVKRQ
HDIVSSN
//
