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Database: UniProt
Entry: A0A364NAS0_9PLEO
LinkDB: A0A364NAS0_9PLEO
Original site: A0A364NAS0_9PLEO 
ID   A0A364NAS0_9PLEO        Unreviewed;      1421 AA.
AC   A0A364NAS0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=GIDA-domain-containing protein {ECO:0000313|EMBL:RAR14366.1};
GN   ORFNames=DDE83_002316 {ECO:0000313|EMBL:RAR14366.1};
OS   Stemphylium lycopersici.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Stemphylium.
OX   NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR14366.1, ECO:0000313|Proteomes:UP000249619};
RN   [1] {ECO:0000313|Proteomes:UP000249619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA   Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT   "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL   Submitted (MAY-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}.
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:RAR14366.1}.
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DR   EMBL; QGDH01000023; RAR14366.1; -; Genomic_DNA.
DR   STRING; 183478.A0A364NAS0; -.
DR   Proteomes; UP000249619; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   CDD; cd04496; SSB_OBF; 1.
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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000424; Primosome_PriB/ssb.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
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   Pfam; PF00436; SSB; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM01228; GIDA_assoc_3; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
DR   PROSITE; PS50935; SSB; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00252}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW   WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT   REPEAT          79..113
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          190..232
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          303..334
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          1313..1384
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..70
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1421 AA;  155417 MW;  27979A3254475DDE CRC64;
     MDFSAGEDED LKQYMPSQFG KKDGGVDVEA QIERARRKVV DESKQAKEKG GSDDEKDSDD
     DSDMSDEEDE FPVSHELIIK THDRAITTIA LDNSGTRLVT GSNDCTLKLH DLSALTPSTI
     RAFKTVDPFA TKPSQTAESH SIHQVLFGPH SGGQFLCITA TSQARLFSRD GDLISEFVKG
     DMYLRDKHNT KGHTAEVTSG AWHPTNRDRF ATAGTDSTVR IWDVNKRMKQ EEVIVHKSRA
     AGSAGMTRMT AIAWGAAAEG GSSMLVSAAL DGSLVMWGGE GPYHRPTAEI KEAHAKDTWT
     SGIDISSDGR LVVTRGGDDT IKLWDTRKFK TPLNTASHPS TSSQFPTSNI KFAPNMQSII
     TGSETGHLHI LNPATLRPEL VTPVTPGSPL ITVNWHPRLN QILTGSANGQ TTILFNPKLS
     NAGALTILSK APKKRHVDDD PSLTVDMDPL GMAGEAHDPS GNAASFSARH PTIGLTASGK
     SRDPRRPHIP ATTPFAKSTP DQKYVMEQIE GSDMRDEDPR EALLKYAPKE GEKAIFTGAW
     EKTQPVGIYK DYDTQQLSPT PPPLIKPPQL SLFRRRPPLS DPAKMFTSTF RAAARAPLSA
     SAFARSFSST RPSQIARMTV VGRLGVAPEE VTVSGERTLV RYVVGTSYGK GEDKKTSWFR
     VASFVQGAQK DFLMSVPKGS LLYVDADARM ETYLDAEGNK KSNLSLVARN FDVLSRPRSE
     EPETNDEDMQ RIVPLPARQL WGHAPRVRAI RPFNRIRRTF ATVSSAERPY DVIVIGGGHA
     GCEASAAAAR AGARTALVTP SVENLGVCSC NPSFGGIGKG TMLREIDALD GVVGRIVDKA
     GVQFRVLNRK KGPAVWGPRA QIDRALYKRY MKDEMLTYKG LSVVEGKVAD IIVDQTQEEG
     CKGTYGKITG VRLESGEIIP TGNVVITTGT FLGGEIHIGL EAYPSGRMGE AATTGLSKSL
     REAGFTLGRL KTGTPPRLDG KTINYKVLEA QEGDDPPMPF SYLNDRVQVE DQLLNHETRT
     NEATHDVIRK NLDKSIHIRE TVKGPRYCPS LESKVIRFAD KTSHIVWLEP EGFDSDMIYP
     NGISCTVPAD VQNTMLKTIK GLENVTMLQP GYGVEYDYVD PRHLRSTLET KNISGLFLAG
     QINGTTGYEE AAGQGIIAGI NAGLKSLGKE AMVLTRADGY IGIMIDDLIT KGVSEPYRMF
     TSRSEYRMSA RADNADTRLT AMGRASGVVS DTRWTAFSDE ATQMAALTQI LRSKTLGWTD
     WKQHGFAVRN DSTKRSAYDL LRLPNTTPTS LTSLLPDIKA FSPRIRDRVH IEATYAPYVA
     AQTASQARWL KDESLKLPLD LNYEAIFGLS FEEKRALEIA RPESVGMARR VEGVTPAGAL
     RLLQYVKGVG KEERMARAKE EIEARKERYR GVMPGVGVEG L
//
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