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Database: UniProt
Entry: A0A371CGZ8_9APHY
LinkDB: A0A371CGZ8_9APHY
Original site: A0A371CGZ8_9APHY 
ID   A0A371CGZ8_9APHY        Unreviewed;       259 AA.
AC   A0A371CGZ8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Glucose-inhibited division protein A {ECO:0000313|EMBL:RDX39552.1};
DE   Flags: Fragment;
GN   ORFNames=OH76DRAFT_709413 {ECO:0000313|EMBL:RDX39552.1};
OS   Polyporus brumalis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Polyporus.
OX   NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX39552.1, ECO:0000313|Proteomes:UP000256964};
RN   [1] {ECO:0000313|EMBL:RDX39552.1, ECO:0000313|Proteomes:UP000256964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX39552.1,
RC   ECO:0000313|Proteomes:UP000256964};
RX   PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA   Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA   Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA   Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA   Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT   "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT   exposes the biotechnological potential of its oxidative enzymes for
RT   delignifying raw plant biomass.";
RL   Biotechnol. Biofuels 11:201-201(2018).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KZ857755; RDX39552.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371CGZ8; -.
DR   STRING; 139420.A0A371CGZ8; -.
DR   Proteomes; UP000256964; 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; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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   PRINTS; PR00411; PNDRDTASEI.
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:UP000256964}.
FT   DOMAIN          31..257
FT                   /note="MnmG N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01134"
FT   NON_TER         259
FT                   /evidence="ECO:0000313|EMBL:RDX39552.1"
SQ   SEQUENCE   259 AA;  27542 MW;  F4DF132A5AAD092C CRC64;
     MHRCIARAVT KSFRSRHYAT ISQATDPQHY DVCVIGGGHA GCEAAAASAR TGARTLLLTQ
     NLSTIGELSC NPSMGGVGKG TLMREVDALD GLCSKVTDEA GIQFQILNRS KGAAVWSPRA
     QVDRKLYRRH MQAALHSYPN LDIHAGSVFD LVLKQPDVSA QLPRAEVAGV KLDSGEVITC
     SQVVICTGTF LSGEIHIGMR RFPAGRMNEA PSVGLSASLD AAGFRLGRLQ TGTPARLAKD
     SIDFSKLDVQ IGDAAPLPF
//
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