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
//