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Database: UniProt
Entry: A0A178E2K2_9PLEO
LinkDB: A0A178E2K2_9PLEO
Original site: A0A178E2K2_9PLEO 
ID   A0A178E2K2_9PLEO        Unreviewed;       664 AA.
AC   A0A178E2K2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=FAD/FMN-containing isoamyl alcohol oxidase-like protein MreA {ECO:0000313|EMBL:OAL50206.1};
GN   ORFNames=IQ07DRAFT_49207 {ECO:0000313|EMBL:OAL50206.1};
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:OAL50206.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL50206.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL50206.1,
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 oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; KV441645; OAL50206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178E2K2; -.
DR   STRING; 765867.A0A178E2K2; -.
DR   InParanoid; A0A178E2K2; -.
DR   OrthoDB; 1641938at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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:SF91; FAD BINDING DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_6G12070)-RELATED; 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:UP000077535};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..664
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008085041"
FT   DOMAIN          182..361
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   664 AA;  72598 MW;  B2131D09532C4135 CRC64;
     MAFNNWNFRH LASSIVLITP VITAQSIAPA HTIVPTKTAA NVPLLPVETL QFTDAVLERI
     GKDNATAQIA NVFAFDSNST TPGRNLTACK TFPGDAFWPS ASNWETFNAL LNSGLVPTVP
     IGAPCYNSQW GQKDIARCNA IVSAFTRPLT HEDDPTSIMW PIYQGKTCMA RNDTSAADTC
     TLGAFPEFAV NVSSVAQIQL AVNIARNLNI RLVIKNTGHD YLGKSSGAGS IGIWMHNIKD
     IVFLPNYEFE GYSGNAFKVG AGVTLEEIYK AASANGVTVL GGICPSVGYA GGYLQGGGHT
     PLSGFHGMGA DAVLAFQVVT ADGRFITASK TSYPDLFWAL RGGGPGTWGV VTSAIVKVYP
     ETDVTLSTYV LGNSTDGTQL VSRESFFKAL RVLWQSFPAW TDANTYSFFF VFNTNGQLTL
     DMRNFFAPGH TPESLEKLKK PFFDIVKDLG IPFQKPKNTT YYPTYLPAYM DAWGKNSFPL
     GLTTSLPGNR LVPRVLWETP ESFEILWKTV VNHVERGHHF GVYHQAPGNP QNADNAVSSA
     WRNAQSFFIT KTPNFPANAT AQEMAAANRV LNEDNLQPWR DIAPASKGGG SYMNEANVEE
     PRWKEDFYGE QYERLVQIKK KYDPKGLFYA MTGIASDEWE VRDVDLGVKT QNGRLCRVGV
     EGSG
//
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