ID K2S018_MACPH Unreviewed; 490 AA.
AC K2S018;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Glucose-inhibited division protein A-related protein {ECO:0000313|EMBL:EKG15834.1};
GN ORFNames=MPH_06973 {ECO:0000313|EMBL:EKG15834.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG15834.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG15834.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG15834.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG15834.1}.
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DR EMBL; AHHD01000291; EKG15834.1; -; Genomic_DNA.
DR AlphaFoldDB; K2S018; -.
DR STRING; 1126212.K2S018; -.
DR VEuPathDB; FungiDB:MPH_06973; -.
DR eggNOG; KOG2311; Eukaryota.
DR HOGENOM; CLU_007831_2_2_1; -.
DR InParanoid; K2S018; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000007129; 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; 2.40.30.260; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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; 2.
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:UP000007129}.
FT DOMAIN 366..437
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 490 AA; 54632 MW; 08A42D1541F181B6 CRC64;
MGEAATFGLS KSLREAGFKL GRLKTGTPPR LDRKTIDFSA LEPQPGDEPP MPFSYLNDRV
QVEDQLFCHS TYTNDATHDI IRANLDKSIH IRETVKGPRY CPSLESKILR FGHKERHIIW
LEPEGFDTDV IYPNGISMTV PADAQAAMLR TVKGLENVTM LQPGYGVEYD YVDPRNLRST
LETKNIKGLF LAGQINGTTG YEEAAGQGVV AGINAGLSAQ GKAPFSLTRA DGYIGIMIDD
LVTKGVTEPY RMFTSRSEFR MSARADNADA RLTAKGRAAG VVSDKRWRVF EDTANQMAEL
TKYLQSQVAG SNHWMARGFR VREDTTKRSA FDLLRLADVT TATLEPMFPE IRYYDPKVRE
RVDIEGVYAP YVEQQKAAMR VFLKDENLRL PADLDYEGIH GLSFEEKQML KQARPESVGQ
ARRIEGMTPN GALRLLAFVK GEARAKARER ALQEVEANRR DRGEKDVGGI EGLEGLEVIE
GVDGQAEATR
//
