ID A0A0N4UAS9_DRAME Unreviewed; 652 AA.
AC A0A0N4UAS9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
GN ORFNames=DME_LOCUS8158 {ECO:0000313|EMBL:VDN58185.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000427501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000427501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN58185.1, ECO:0000313|Proteomes:UP000274756}
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}.
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DR EMBL; UYYG01001166; VDN58185.1; -; Genomic_DNA.
DR STRING; 318479.A0A0N4UAS9; -.
DR WBParaSite; DME_0000427501-mRNA-1; DME_0000427501-mRNA-1; DME_0000427501.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; 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 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000274756}.
FT DOMAIN 562..637
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 652 AA; 73827 MW; 8A4F82A277C43404 CRC64;
MKHSRLLTNA VKLFDVIVIG GGHAGCEAAA ASARSRARTL LLTHRKETIG EMSCNPSFGG
IGKGHLIREI DAMDGLCARI CDKSAITYQA LNTGQGPAIL GLRAQIDRDL YKKYMQEEII
CGTPNLTVIE GSVGDLIIEN STKPECIKVS GVILENGQMI RSNAVVVTTG TFLDGEVFWG
LKRFPYGRLG EKACTKLSQK FSQLGFKIGR LRTGTPPRLL KKTIDFSKFE LKPADKNPIP
FSFLTKTLWI DPDKQLPTYL SYTNDRVAEL VRKHYKEHKY IRSEQIGPRY CPSLESKIIK
FENVYHKFFL EHEGLESELI YPQGMSMTFA EDVQREIMRS IPGLENVEIA QAGYGVEYDF
INPQQLHSSL ETKLVKRLFL AGQINGTTGY EEAAAQGNNF IASILAGINA AAVTRGIKPL
LLDRTEAYIG VLVDDLTSLG TNEPYRMFTS RAEFRLHLRP DNADIRLTDK AYHMGVVSED
RYSHFLNLKT RLKDATELLK SIKYPLATWP KYLQNFKPKN KLGKVYTAYD LLHRHDISFR
ELERAFPKEM SPFLDNELES RIRIEGLYKK QHDLLVEKMI TVRREGRALI PENIKYSNID
GLSFECMEKF EQWRPQNLAA ASRVPGVTPE ALYILLRYIK TPEIQKHCCV GD
//
