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Database: UniProt
Entry: A0A2N3NB53_9PEZI
LinkDB: A0A2N3NB53_9PEZI
Original site: A0A2N3NB53_9PEZI 
ID   A0A2N3NB53_9PEZI        Unreviewed;       482 AA.
AC   A0A2N3NB53;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Amine oxidase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=jhhlp_004246 {ECO:0000313|EMBL:PKS09627.1};
OS   Lomentospora prolificans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX   NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS09627.1, ECO:0000313|Proteomes:UP000233524};
RN   [1] {ECO:0000313|EMBL:PKS09627.1, ECO:0000313|Proteomes:UP000233524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS09627.1,
RC   ECO:0000313|Proteomes:UP000233524};
RX   PubMed=28963165; DOI=10.1534/g3.117.300107;
RA   Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA   Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT   "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT   prolificans (Formerly Scedosporium prolificans).";
RL   G3 (Bethesda) 7:3831-3836(2017).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00043981}.
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:PKS09627.1}.
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DR   EMBL; NLAX01000010; PKS09627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3NB53; -.
DR   VEuPathDB; FungiDB:jhhlp_004246; -.
DR   InParanoid; A0A2N3NB53; -.
DR   OrthoDB; 1771364at2759; -.
DR   Proteomes; UP000233524; Unassembled WGS sequence.
DR   Gene3D; 1.10.405.20; -; 1.
DR   Gene3D; 3.30.70.1990; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR42923:SF26; FMN REDUCTASE LOT6, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06600)-RELATED; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233524};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..482
FT                   /note="Amine oxidase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014781522"
SQ   SEQUENCE   482 AA;  52533 MW;  A2C769260726CB5C CRC64;
     MAPLRLFATL NILGATGVAL GAINKCSFPA NRTIQRDVAI IGGGASGAHA AVLLKEDYGK
     SIVVVEKQGR LGGHVATHED DNGNTYEYGV QSYLDYGEAL AFFERFNVTT GTPARVPLTS
     VYADFSTGLN VTDFVAPAND ARLEALTRFL EAVAPYEDMI LPGYWNFPAS EDIPEDLLIP
     FGEFAKKYDL DAAMPQMFQV PGPGVPDWTE APTLHVIQVF GAPMARALSG QLAGFAPTSH
     NNTELYGKIG DLLGDDVLYL STVVETKRDD NGVELVVQSE SGEEYLIVAK KLLVAVEPTV
     ETMQPFDLDN DEWAVFEKFD YSTVYAGIVS HPSLPVNVSL VNTVPEAAPA NYYQFPQGPI
     LARFDYMGSD SDYFRVLIVG DRDFDEAGAQ ILVRDSIANL IDGGALPEGD IDDVDYVAFV
     NHGPMHLRAS VEAIEGGFIQ EQYALQGRRS TWYTGAAWSV QFTTILWAFN DVLLPKVVED
     LE
//
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