ID A0A0G2DUJ1_9PEZI Unreviewed; 722 AA.
AC A0A0G2DUJ1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Putative l-amino-acid oxidase {ECO:0000313|EMBL:KKY14632.1};
GN ORFNames=UCDDS831_g08116 {ECO:0000313|EMBL:KKY14632.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY14632.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY14632.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY14632.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY14632.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY14632.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KKY14632.1}.
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DR EMBL; LAQI01000219; KKY14632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2DUJ1; -.
DR Proteomes; UP000034182; 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;
FT DOMAIN 239..694
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 722 AA; 79984 MW; 2F32056C6B26F712 CRC64;
MGRQGLKTSR VEPTKSPIHS RVDLLDITKA GRCSPVGERR WARHIFGLPL PAAHYVNHAF
PLQSGLIAAS CFVAPLAKPS TTVVFKGPFV AEADGITNIH IDFAGPIDGE LSVHYGSCDI
ASPYEAHHRV GKTHLGNHPL AKRNLGWEDN RPTRFVWLPP AEIQSGGCLH AFAGDELVGR
SDAFKVKRRK ARRSTSFADI ADPMGPWFDG VEYLKEKEPG SAFVAQAMNK SVGIIGGGMS
GLMTAYLLES VGITNWKIIE ASERIGGRVH TSYLNDTAPE DYQYQEMGPM RFPVSLTNTT
TNDTIQIMDH RMVFQLADAL NEMNGHDPAW SVDFIKWIQK SANDPVDSTD ATLSYSNATA
VENALEAIED WDALTWEKMR DIATNVFDAH KKAVAEGYFD FSEAGYLRYK LQTDLNVTDE
AVSTASDNPE WLYDTVYFSA TEWRTIDKGL SRLPKAFTPL VANRTLFGKQ VEQLSYNETT
QQTTASWRPD GPWGTTLDSL SFDYAVVAVP FSKVRLWDLP SYSGLLARAI STLNYEQSCK
VALHYETRFW EHLSPPIIGG CGSTSAWAGI GNICYPSYQV NSTGPGVLLA SYQSGTIART
LGSMTEAEHV AHVVRAMTAV HGDVATEQFT GAYDRICWEN NNFQAGAWAS PLVGQQELYL
PAYYQTEHHT VFVGEHTSFT HAWIWSALES AVRGTTQLLL EMGLVDEAKQ VTETWMARWM
HV
//