ID A0A178DSN3_9PLEO Unreviewed; 664 AA.
AC A0A178DSN3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=FAD-binding domain-containing protein {ECO:0000313|EMBL:OAL46614.1};
GN ORFNames=IQ07DRAFT_156136 {ECO:0000313|EMBL:OAL46614.1};
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:OAL46614.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL46614.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL46614.1,
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; KV441654; OAL46614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DSN3; -.
DR STRING; 765867.A0A178DSN3; -.
DR InParanoid; A0A178DSN3; -.
DR OrthoDB; 1641938at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR13878:SF171; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-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 SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..360
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 664 AA; 73359 MW; 96295D6E2261515E CRC64;
MDTNERRPLL DEKFVQIDGV ERNAVGEYAH KRRTERWRKI SLSLICGFAL YGSFSFFNGH
RTQHSHSDTS NQTPFHGAVV SNYTCVPGHS CWPSANEWIS FNQSIHGNLR LTVPWAAPCY
SSPSSKACQD VVKNYADGTS RTAQYGAMEF LDWETCGESQ CFLNSHNPSS PVSGNCSLGR
LSTYHVEARS ASDIAVTLDF VRVHGIRVSI KNTGHDYFGR SNAANSLAIW THNMKDMAFH
KEFQPKGCSA RYENIAEVGA GVQAQEAWTF FEPLNMLVTV GAVGSVGIAG GFGQAGGHGP
LGPSYGLMVD QAVEFEVVTA DGQKRTINEC TDPDLFWAMR GGGGGNYAVL TSYKFQLHPA
VPLNVYSFQA KFLLPDGDLD IAESKVHRDV VRSLASNQLD FAKYGIAGYN FLLPDHMVSL
QVMPSSDTEA IKTITSDWHD FLNTHPDLNV TESSYYSFPK FSDWHRFTEM PAIAGNGPVG
LGIMEAGRFI PKDLFESPDD IEKVVNAVVT AMQFSKSNGG GGSAQLYATG PVNHPDNSKT
GVNPAWRTTL WHVIMGAGWT KNTSPEMRTR IQNTISASVQ PFKALTPGGG CYMNEGDWME
ENWEHTFFGE NYDRLLAVKR RYDPSGLFNC WKCVGWTGYD DSMYSCYTQS RKQPHPTIPL
GPVS
//
