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Database: UniProt
Entry: A0A1L7XC03_9HELO
LinkDB: A0A1L7XC03_9HELO
Original site: A0A1L7XC03_9HELO 
ID   A0A1L7XC03_9HELO        Unreviewed;       574 AA.
AC   A0A1L7XC03;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Related to L-amino-acid oxidase {ECO:0000313|EMBL:CZR62559.1};
GN   ORFNames=PAC_12456 {ECO:0000313|EMBL:CZR62559.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR62559.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR62559.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR62559.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FJOG01000021; CZR62559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7XC03; -.
DR   STRING; 576137.A0A1L7XC03; -.
DR   OrthoDB; 3597164at2759; -.
DR   Proteomes; UP000184330; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.20.1440.240; -; 1.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR10742:SF342; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000184330}.
FT   DOMAIN          97..546
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  64067 MW;  F95D9DAA8C795EBD CRC64;
     MLPAHLTFNQ HTTNSSPRNP RLQRPSHRGS SRHSQHSHQL HPPPLRPPLP PLRLLLFIGD
     AEGPWFDGVE YLSAKEPSET FVAEAKTKSI GILGAGMSGL MSALLLESVG FHDWKIIEAS
     SRLGGRVHTA YLDNTTGAEY QYQEMGPMRF PVDLTLGNET VEINDHKMVF QLADVLNEMN
     GNSSEYMVNF IKWIQSNSNA PKSNSTTTYS NLTAVTAASD GYDNFMNLTN DKLFAAAQNV
     FTAHRSAVDA GILDFSESGY IKYVLGASND ITDEIDTLSD NYDSWYYDSV YFSASTWKTI
     DQGLNRLPLA FTSLVENRTM FGTAIQEISY NETTDKVTVG YRPDPFQQEA DTIDFDYVIT
     AVPFTKVRLW RLPEYSSLLQ RAINTLQYET ACKVALKYET RFWEHLDKPI FGGCGSTSIP
     AIGSICYPSY NLNASGPGVL LGSYISGTTC QSLGALTDIE HVSLVQRAIV EIHGQVASDQ
     FTGSYNRKIW ANDEFQAGDW AAPAAGQQEL YLPAYFRTEF KTIFVGEHTS YTHAWIWSAL
     ESAVRGTVQL LLDMGLVDEA KQITEEWMAR WIQV
//
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