ID W7MPJ5_GIBM7 Unreviewed; 681 AA.
AC W7MPJ5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme GidA {ECO:0000313|EMBL:EWG49699.1};
GN ORFNames=FVEG_09153 {ECO:0000313|EMBL:EWG49699.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG49699.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG49699.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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; DS022253; EWG49699.1; -; Genomic_DNA.
DR RefSeq; XP_018755890.1; XM_018898084.1.
DR AlphaFoldDB; W7MPJ5; -.
DR STRING; 334819.W7MPJ5; -.
DR GeneID; 30066831; -.
DR KEGG; fvr:FVEG_09153; -.
DR VEuPathDB; FungiDB:FVEG_09153; -.
DR eggNOG; KOG2311; Eukaryota.
DR OrthoDB; 49088at2759; -.
DR Proteomes; UP000009096; Chromosome 5.
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:UP000009096}.
FT DOMAIN 579..650
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT REGION 660..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 75474 MW; 2222CEFF159F7839 CRC64;
MRALLRPRAA VLRHQWIITR RRYLATVSSD LRPYDVVVIG GGHAGAEACA AAARSGARTA
LVTPKIDNLG TCSCNPSFGG IGKGTIIREI DALDGLAGRI IDKSGVQFHT LNRRKGAAVW
GPRAQIDREL YKKHMKDELS SYPGLSIVLD SVSDIVTEPQ ELFEGASSRI AGVRLESGQT
LPTKKVIITT GTFLGGEIHI GLTAYPAGRL GEAATFGLSK SLRDAGFELG RLKTGTPPRI
DAASINYDVL EKQYGDDPPT PFSYLNETVA IREQMTCSVT YTTEETHRIV RENLDKTIHI
RETVKGPRYC PSLESKIIRF ADKERHIVWL EPEGLDSPVI YPNGLSMTIP AEAQEEVLRT
IPGLENSKML QPGYGVEYDY IDPRGLKSTL ETKAISGLYL AGQINGTTGY EEAAGQGVLA
GINAGRSSQG FPQVFLSRGD GYIGIMVDDL ITKGVTEPYR MFTSRSEFRM ASRADNADVR
LTSKGYGWGV ISEKRWSRFR DERQQIDDLT KLLQSVSLSP LQWIEKGYHM KRNTQRRDGI
DVLRLSNPDT RVGIEQLAPV IPGVMDFPPR VRRRVEIESF YAPYIKIAES ERKQLTNDER
VKIPLDLNYD NIPGLAMSEK EALKAAKPEN LAQARHVEGV TPSGSLRLLA HVRRRPEAYL
LEKDASRGRR TQRTNKNRGS V
//
