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Database: UniProt
Entry: R1GSU8_BOTPV
LinkDB: R1GSU8_BOTPV
Original site: R1GSU8_BOTPV 
ID   R1GSU8_BOTPV            Unreviewed;       640 AA.
AC   R1GSU8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Putative flavin-binding monooxygenase-like family protein {ECO:0000313|EMBL:EOD51326.1};
GN   ORFNames=UCRNP2_1917 {ECO:0000313|EMBL:EOD51326.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD51326.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004721}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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DR   EMBL; KB915882; EOD51326.1; -; Genomic_DNA.
DR   RefSeq; XP_007581228.1; XM_007581166.1.
DR   AlphaFoldDB; R1GSU8; -.
DR   KEGG; npa:UCRNP2_1917; -.
DR   eggNOG; ENOG502SHCE; Eukaryota.
DR   HOGENOM; CLU_006937_8_2_1; -.
DR   OMA; HIAYIIA; -.
DR   OrthoDB; 2785305at2759; -.
DR   Proteomes; UP000013521; 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; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR43098:SF2; FAD-BINDING MONOOXYGENASE AUSB-RELATED; 1.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 3.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:EOD51326.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521}.
SQ   SEQUENCE   640 AA;  70554 MW;  8B97D521619E14C8 CRC64;
     MAGSISLEAP QAGPDPKVLQ KYEEERQKRV REDGQSQFID LDKTDRFKYL GDDPWVDHDA
     LNAQEPPLSD GSQCQFLIYG AGFGGLCYAV RLIEAGFCVE DICIVDTAGG FGGTWYWNRY
     PGLMCDVESY IYLPLLEETG FMPKHKYSYG PEIRGHAERI ASKWNLKALF RTQVKSQTWD
     ESRKQWAVNM TEGRGPGQEA RDLQVHSNFV VIAGGILNVP HIPKLAGLED FKGQHFHSSR
     WDYKITGGSE HDQQLTELKG KRVGFIGTGA TAVQAVPVLA KYAKELYVFQ RTPSACDTRG
     QRETTPEDWK KIAYRPGWQR ERRENFNSFI FGNPEGTENL VNDGWTTFPS YQVVLGGPLL
     APSDIPAHID RMNALDFPRS ERVRARVDAL VKDPATAASL KAYYPGWCKR PTYHDEFLQT
     FNAPHVHLID TAGAGISHLT PTSVVANNTA HPIDILILGT GYRPPMPGSW ALNAGGVKVT
     GRDGLDMDGK WAAVGAATLH GVAAHGFPNL LLWSPTQTGM TANAVAVADD VARHAAYVVR
     EARRRAGGVD AFALQPSREA EEAWATESAA RAAWFAPLFG CTPSYLNMEG DAERRMAAGG
     EEERAKAGRA AHWAGGAAEY NARIKAWRDE GGMQGIEIWT
//
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