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Database: UniProt
Entry: A0A2G8RPR5_9APHY
LinkDB: A0A2G8RPR5_9APHY
Original site: A0A2G8RPR5_9APHY 
ID   A0A2G8RPR5_9APHY        Unreviewed;       491 AA.
AC   A0A2G8RPR5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GSI_14816 {ECO:0000313|EMBL:PIL23504.1};
OS   Ganoderma sinense ZZ0214-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Ganoderma.
OX   NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL23504.1, ECO:0000313|Proteomes:UP000230002};
RN   [1] {ECO:0000313|EMBL:PIL23504.1, ECO:0000313|Proteomes:UP000230002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL23504.1,
RC   ECO:0000313|Proteomes:UP000230002};
RX   PubMed=26046933; DOI=10.1038/srep11087;
RA   Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA   Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA   Li X., Schwartz D.C., Wang Y., Chen S.;
RT   "Chromosome-level genome map provides insights into diverse defense
RT   mechanisms in the medicinal fungus Ganoderma sinense.";
RL   Sci. Rep. 5:11087-11087(2015).
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:PIL23504.1}.
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DR   EMBL; AYKW01000068; PIL23504.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8RPR5; -.
DR   STRING; 1077348.A0A2G8RPR5; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000230002; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230002}.
SQ   SEQUENCE   491 AA;  55138 MW;  AA3A87D4EE8022D9 CRC64;
     METNPHRLPE VSGAEPSAKH ICIIGAGPTG LGALKIVKDA PQFKEGRWKV TAFEAREKIG
     GIWLPAPADA DPPLTALYDS LTANTPHPLM CYSSYLFLPA TPLYPRAKVV LDYIEDYARH
     FDLNQHIRLN TSVLAVHWDA SSSKWDVTVS GKGGEETIGF DLVLVANGHF RVPRIPEVKG
     LAEWIAKGKV THTAWYRRPE NYTGKLLVIG GGYSGQDVAS ETRPYAKEVI HSITRVAPED
     KDGGKFKRRG RVAEYLDPDK GNVLFEDGET MTGVDYVVLA TGYQFNFPFL SEPEVLPSIP
     PRVPPIPPVL HNSTYHIFPM AKHMFPLVTA YPPSSIAFLG LPLRVAPFPM TEIQTRAALK
     VFADPTALDM EREAAALDAR YRQFRGTQDR DEVAIADAWF RFDFDEMFDY RDELHEFMGD
     TFRVPEWERR LFEQKDALRE QWRELERLGE ADGWSKGVGA GTDPWQEWAD FMSKVLRRAP
     AGEEVSSNST S
//
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