ID A0A177C690_9PLEO Unreviewed; 497 AA.
AC A0A177C690;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=CC84DRAFT_1096824 {ECO:0000313|EMBL:OAG03045.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG03045.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG03045.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG03045.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|RuleBase:RU362067}.
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DR EMBL; KV441555; OAG03045.1; -; Genomic_DNA.
DR RefSeq; XP_018033410.1; XM_018174683.1.
DR AlphaFoldDB; A0A177C690; -.
DR STRING; 1460663.A0A177C690; -.
DR GeneID; 28758169; -.
DR InParanoid; A0A177C690; -.
DR OrthoDB; 5471885at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR Gene3D; 3.90.660.10; -; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR10742:SF218; AMINE OXIDASE; 1.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 48..479
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 497 AA; 55308 MW; A0C6DD7B417FA38E CRC64;
MTSRDGFTWT PSDGLKPGVP SLGVISPSSN ISSTQVEYDV IVIGAGYCGL TAARNAALDG
LKVLLLEGRD RIGGRSWSSN IGGYPFEMGG TWVHWGQSNS WREITRYRME KDVEMSFDFA
KGVKHFELNT PESSVTMTHD DEDILLDSAL KKFTNIDGFY GRKTIPLPYT TFHQPSSIPL
DSLSALDRIN EIADTLSPQE RAVLEASILL ASGGTLETTS FHEFMHWWAM CGYTYQGWLD
MLITWKFRDG QSTFARRFFD EALATKRLSY AFNTPVQHIS TSPSAVEITS RSNTTYRALR
AICTIPLNVL SDIKFTPPLP TGKQAAIAIG HVNQTVKVHA EVSNKDLRSW TGINYPNELH
YAIGDGTTPA GNTHIVCFGG QNRHMDPEVD VDRTKRAVSS LFNPGNYAGQ NVQIERLVFH
NWSKDEFAKG AWFFAPPGLL SEHLDDMRGR HGNVVFANSD WALGWRSFID GAIEEGTRAE
LEVREEVVGL RGVKQKL
//