ID A0A178ADQ6_9PLEO Unreviewed; 436 AA.
AC A0A178ADQ6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:OAK95408.1};
GN ORFNames=IQ06DRAFT_352441 {ECO:0000313|EMBL:OAK95408.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK95408.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK95408.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK95408.1,
RC ECO:0000313|Proteomes:UP000077206};
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; KV441722; OAK95408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178ADQ6; -.
DR STRING; 765868.A0A178ADQ6; -.
DR InParanoid; A0A178ADQ6; -.
DR OrthoDB; 1422702at2759; -.
DR Proteomes; UP000077206; 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; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF187; MONOOXYGENASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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:UP000077206}.
FT DOMAIN 17..44
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 122..377
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 436 AA; 48600 MW; 3AE9E9A7E80909A6 CRC64;
MAAQQANGTK PKTGIKVIII GAGFGGLTAA IECVRQGHSP VIYESFPSLK ILGDIITFGP
NAGRIFTRWD NGSVAAKMRK ISIDLQSYGF NIHKYDTGEI VLNQKNPPRD ETSPMFNGHR
GELHEIVFEY AKSVGVEINL GQRVQKYWEN DDKAGIELED GTKVEGDVVI GSDGVRSKAR
TLVLGYEDQP KSSGYAVWRA WFPNKDMIAD PETRQFCENG DTFNGWIGPD VHFLFSTLKG
GSDCCWVLTH RDEHNIDESW SFPGYLKDVK EVLEGWDPMC WKIVSKTPED KLVDWKLVYR
DPLPNWVSGY GSAPGHGRIC LLGDAAHPFL PTSAQGATQA LEDGVTLAVL LRQAGKGNVR
GALRAYQDVR YERVKAVQKT GETTRDKWHN TDWDAVKKDP TLIQFPREDW IFKFDAETHV
EEVGEEAVKK ATVALA
//
