ID A0A2H3BVE1_9AGAR Unreviewed; 576 AA.
AC A0A2H3BVE1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=GIDA-domain-containing protein {ECO:0000313|EMBL:PBK74795.1};
GN ORFNames=ARMSODRAFT_950847 {ECO:0000313|EMBL:PBK74795.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK74795.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KZ293418; PBK74795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3BVE1; -.
DR STRING; 1076256.A0A2H3BVE1; -.
DR OrthoDB; 1594646at2759; -.
DR Proteomes; UP000218334; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR040131; MnmG_N.
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; PF21680; GIDA_C_1st; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000218334}.
FT DOMAIN 27..407
FT /note="MnmG N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01134"
FT DOMAIN 472..561
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal N-terninal subdomain"
FT /evidence="ECO:0000259|Pfam:PF21680"
SQ SEQUENCE 576 AA; 63780 MW; DDF4B3147BBAAC9F CRC64;
MFPHLTRQPW NRLRLHRYFS SATEPYQVCV VGASHAGCEA AAASARVGAR TLLLTKSLDD
IGELSSDPSI GGIGKGILVR EVDALDGLMA KVADKSGSMF QMLNVTKGSA VWGPRAQIDR
TLYKRQMKRE LRRYQQNLYI RAARASSLLV DSEPHDLHVS GVKLDTGEII HCSKAVLCTT
REYRIGTTGD DDFEDLWSSL RRLGLEFHQS HTITQPRLDG KTINFTNLTR QDGDVSPSPF
SFLSSAVANA ENQIPRYMTR TTSATHDIVR DNMHLSALIE EASGSRHCPT LEAKSLRFSH
NSLPVWLESE GYDTDVVCAN GLACTLPEEV QGPMLRTIPG LENVKMLSPA YGIKYDYLDP
RILTETLEEK HVKGFYCAGK PAGTPGYEEA AGQGIIAGAN AARSALGRGP FLLKRSESFI
GSLTHDLITR GVPVPQSTSP PRSDYRLFVR PDNAHIRMTA KAYGAGVISR GRMESHSRLL
ETYNRVLRML KHCIRNAHSW HARGHSVAHS NKKKSAFYLL RLPSVSMAGL IREFPLLKDV
DSRLLKVVEH DGKYAPHLAR ARLDMKAMSK NGLDPD
//
