ID A0A0L1J539_ASPNO Unreviewed; 627 AA.
AC A0A0L1J539;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Metalloreductase {ECO:0000313|EMBL:KNG86523.1};
GN ORFNames=ANOM_005229 {ECO:0000313|EMBL:KNG86523.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG86523.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG86523.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG86523.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000256|ARBA:ARBA00006278}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNG86523.1}.
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DR EMBL; JNOM01000112; KNG86523.1; -; Genomic_DNA.
DR RefSeq; XP_015407446.1; XM_015550486.1.
DR AlphaFoldDB; A0A0L1J539; -.
DR STRING; 1509407.A0A0L1J539; -.
DR GeneID; 26807033; -.
DR OrthoDB; 2787294at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IEA:UniProt.
DR GO; GO:0000041; P:transition metal ion transport; IEA:UniProt.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR PANTHER; PTHR32361:SF12; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14340)-RELATED; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 323..472
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 627 AA; 70272 MW; D1B03F799A94F565 CRC64;
MDDLRRHITP RGFGTNATYV YEFSRGLGGV NVPRDVIITR IIYVSVLALA FVVFCGRFAQ
ISHAYLRHIT SLNSSKRQQT YWSVEESDTW TNIKKHLLYS PLGRKRHNRE IQLSSAINVG
TLPSRFQTIL ILLYVASQVA YCTILDYRVN EKKALIAELR GRSGTLAVLN MVPLFLLAGR
NNPLISILHI SFDTYNCLHR WLGRIVVIES VVHTFAWAVN AAEEVSVSDM LKRLCDEPFF
TWGLVGTVAL VFLSLHSPSP VRHAFYETFL HLHQLAALLA FVGVWLHLDL DGLPQKPWAI
TMAAIWIFDR AARFFRLLYL NISPRKGATK LVVRALPGEA CKVTFHLPKH VHINPGSHVY
TYIPSVSLWM SHPFSVAWVD PCSSVTNAAE PENFAKSPSS TGSMSPSLLE KQPVVDLDDY
MRESQEPTSV SLIVSARQGM TRKLYNKALI APNQTLHLSG YIEGPYRSHV SNMGSYGTAV
LFSAGAGITH HMLYVRDLII RASEGRVATQ KVYLIWSVRS TEHLAWVQEW MDEILRLPGR
REILTIKLFV SKPKSSREIV SPSATVQMFP GRCRPHVVLD EVIPNRVGAT IVSVCGPGAF
ADEVRAAARD NIGKGAVVDF VEEAFTW
//
