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Database: UniProt
Entry: A0A178EFY8_9PLEO
LinkDB: A0A178EFY8_9PLEO
Original site: A0A178EFY8_9PLEO 
ID   A0A178EFY8_9PLEO        Unreviewed;       544 AA.
AC   A0A178EFY8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=FAD-binding domain-containing protein {ECO:0000313|EMBL:OAL54053.1};
GN   ORFNames=IQ07DRAFT_677451 {ECO:0000313|EMBL:OAL54053.1};
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:OAL54053.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL54053.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL54053.1,
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; KV441639; OAL54053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178EFY8; -.
DR   STRING; 765867.A0A178EFY8; -.
DR   InParanoid; A0A178EFY8; -.
DR   OrthoDB; 879734at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
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; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF22; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..544
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008085438"
FT   DOMAIN          99..270
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   544 AA;  59154 MW;  B85D07CB05096681 CRC64;
     MRSVLFPLFC LHLGVYGSAQ GIRGRSYQAS IPAKSNTDRP TTEQCLKILG WKNCKAVDVS
     GSNIQIASNV LTAMIPGAID LPGTEEYNES MTHYWSAAAV ERAASIVHPA SAEEVATTIK
     VLECFQVPFA VRSGGHQTAH GAAAIKDGIL ISLDRLHAIS YNADNEIVSF GPGNRWLSVY
     RHLDIYNRGV TGGHIGLVGT GGQITGGGTS PFFHRYGFSS SNVHNFQVVV AGGSIVNANI
     EENPDLFWAL KGGANNFGIV TRLDMVTFPL QGIWSGGLGF DVGKKEEVLG AFWKFQTESI
     VKDNGTEILL GFGIHGNQSF IRGEAFADSS GYGNESYPDA FKPFYDVGVL YQDAQDQRLA
     VSANLMASEN LPEEGKLWNT PGGEGRMNLA MVTLKPDLQL YSEAVDIYLD TFNAARGVKD
     AQINLHMSPL TANAVRHAKE RGGMAAGWAE EDQLFFNIEM VYSQASDDEL MHSLSRECMV
     KVGALAAERG LLMPTIWMNN AHTEDDVLGS YGAENYAKMK EVSQKYDPKR TFQDLCSGAY
     KLDK
//
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