ID A0A1G4MGU1_LACFM Unreviewed; 686 AA.
AC A0A1G4MGU1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=LAFE_0F17568g1_1 {ECO:0000313|EMBL:SCW02937.1};
GN ORFNames=LAFE_0F17568G {ECO:0000313|EMBL:SCW02937.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW02937.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) 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; LT598490; SCW02937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4MGU1; -.
DR STRING; 4955.A0A1G4MGU1; -.
DR OMA; CNPAMGG; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000190831; Chromosome f.
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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000190831}.
FT DOMAIN 590..661
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 686 AA; 76638 MW; E78A14CB018068F0 CRC64;
MFFHFHLKWS LKLRFPTQCF KRGLVLNAEL KSVLEKLPDS GVIVVGGGHA GCEAAAGSAR
SGTPTMLITP YLNKIGTCSC NPSMGGVGKG TLLREVDALD GVAPKVTDIA GIQFKMLNQS
KGAAVWGPRA QIDREIYLKE MQKVLSSYTN LTLCQGKVQD IIINTENGNN DLENRAYGAV
EGVILEDGRI IKTSKVVITT GTFLRAEIHI GMKSFPAGRI GEDPTYGIST TLKDAGFRLG
RLKTGTPARL DGKTINFKGL EKQYGDKVPH PMSFMNDQVS IKDQVLCYGT QTSPAVHDYL
RANLHRSLHI RETVKGPRYC PSIEAKIIRF SDKHSHKIWL EPEGLSTDII YPNGISNSMP
EDVQERMLRM IQGLEDVKII QPAYGVEYDY IDPRELAPTL ETKLVQGLFL AGQINGTTGY
EEACAQGIIA GINAGLSYQD KNMLTLSRSD AYIGVLIDDL VTKGVEEPYR MFTSRSEFRV
SVRADNADFR LTEIGHHLGV ITDARWQKYL KDKSIYAQIM SELKALEFSA KKWDRLLNIS
VADGAKNRSA WEMLTFHTVD IQKLVDDIPN LQLKIEEIPK HVLMKLNVEG KYAPYIKKQN
QFVKAFQADE NMLLPTTYDY SQINSLSTEC KSILNKVQPL TIGQARRIQG ITPASLFELY
KLVRFKQKEL DLERSKFQTP SDLITD
//
