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Database: UniProt
Entry: A0A178E839_9PLEO
LinkDB: A0A178E839_9PLEO
Original site: A0A178E839_9PLEO 
ID   A0A178E839_9PLEO        Unreviewed;       455 AA.
AC   A0A178E839;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:OAL51479.1};
GN   ORFNames=IQ07DRAFT_566143 {ECO:0000313|EMBL:OAL51479.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL51479.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL51479.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL51479.1,
RC   ECO:0000313|Proteomes:UP000077535};
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   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; KV441643; OAL51479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178E839; -.
DR   STRING; 765867.A0A178E839; -.
DR   InParanoid; A0A178E839; -.
DR   OrthoDB; 1113861at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13789:SF172; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12410)-RELATED; 1.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT   DOMAIN          13..369
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   455 AA;  50482 MW;  29CF1A27C9C392EB CRC64;
     MGSMAHESEW RRLSVAIVGG GIGGMSTAIA LRRAGHEVTI YERNDFAGEA GASVSCAANG
     TRWLHEWGVD VAKGDPVILK KLINRDWKTG EPVSVYDLDD YEEKWGYVYN MFHRQYMHKM
     LMECALQEEG DGTPVKLLVN QSCDAIDLES NVISFSNGAK VQHDLIVGAD GIGSVCRRIV
     GLNPEKRPAE SSCLHANVNT EQVRKLGLVD YSLNSALEYW GGQEGKWDKI VLSPCNGGNL
     LSYYCFFPRS VGDYANHTWG GADLPIEELL APYPELDAQV KAHLAIGVEV QPWRLWVHQP
     YPYIVKNSVA LLGDAAHPMM PHQSQGACMA IEDAAALGIL FNKKYFGGDV RETLAIYQKI
     RLPRATKVQA SAAKAAYNIN ERIGFSSNTT MSNYKVEDEA RKLTIEEMNG YDMYKDVEQA
     LAEKKGEQYN DKYIRGLPFG LELPNGIVID SSWAF
//
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