ID A0A178AL11_9PLEO Unreviewed; 659 AA.
AC A0A178AL11;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=FAD/FMN-containing isoamyl alcohol oxidase-like protein MreA {ECO:0000313|EMBL:OAK98230.1};
GN ORFNames=IQ06DRAFT_357375 {ECO:0000313|EMBL:OAK98230.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK98230.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK98230.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK98230.1,
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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; KV441716; OAK98230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AL11; -.
DR STRING; 765868.A0A178AL11; -.
DR InParanoid; A0A178AL11; -.
DR OrthoDB; 1641938at2759; -.
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; 3.30.465.10; -; 2.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR13878:SF176; FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..659
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008081918"
FT DOMAIN 183..362
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 659 AA; 71731 MW; 1295B4150BF70F5D CRC64;
MSQSARSTRI AIYLYLTLLT IPSLCSAVGL AQNIVSDTIA ANAELFPWER IQLTDVVIDQ
LSHNAATVDL AKVVAFQSNG SDMHRNFTGC KTFPGDNAWP SISTWGEIDS FIGRSLIKTI
PIASVCYYSP WGSKDAAMCN ALVGSFQKFS THEEHPTSIM WPLFQGKTCM ASNTTSSEDT
CTLGSYPEYS VNVSSTAHIQ VAVNLARNLN IRLVVKNTGH CYLGKSTGAG SLGVWTHNLK
DLRFMPGFEL DGYKGPAFKV GAGVTATEMY HAAELHNLTI LGSIAPSVGF AGGYIAGGGH
TPLSGLHGMG ADAALAFQVV TADGRFVTAS ATSNSDLFWA LRGGGGSTFG IVTSVIVKAF
PQTDVSVSSW VLGNSTDGTQ VVSRADFFQA LRIFWEMFPT MTSARTYSFF FIFNTNGQLT
MDMRNFFAPT HTPASLDKLL SPFFAAVKDL GVPLVKAQNT TYYSTFLPAY MQAWGNNNFP
MGTATSIPGN RLLPRSLWDN ATNFERLWNT TVAHIEAGRH FGIYHQAPRN PQGVDNAISS
AWRNCQSFFI THSPSFAENA NSTTIREANR VLVEDNLGPW RKVAPASEGG GSYLNEAAVD
EPLWKEDFYG EQYARLVELK KKYDPTGVFY ATTGIGSDEW ELRGQHLGVT TQNGRLCRV
//