ID A0A1V6S4I9_9EURO Unreviewed; 914 AA.
AC A0A1V6S4I9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=PENVUL_c009G02361 {ECO:0000313|EMBL:OQE08629.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE08629.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE08629.1}.
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DR EMBL; MDYP01000009; OQE08629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6S4I9; -.
DR STRING; 29845.A0A1V6S4I9; -.
DR OrthoDB; 2049651at2759; -.
DR Proteomes; UP000191518; 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:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 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:UP000191518};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..914
FT /note="FAD-binding FR-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012663958"
FT TRANSMEM 320..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 523..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 732..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 611..732
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 62..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 100539 MW; 1DECF0F7FC2EF8B4 CRC64;
MLPRAAFVAL FWASVQVAGH SDSGSSSSSS RNVASNLEEY CFYSIYTSLS AYTFEGSVTV
QSATSGSHSH GGSSSSSHGS SDSSSTEASE TSSHESSDSS TETSETHSHG SSESSSAESS
EASSVAYTHG SSDSSSAESS DSTSGTHSHG SSESSSAESS ETSSVAHTHG SSDASTESSD
STSGTHSHGS SRRSVSLGRR AHGGGSYGSY STGPCNSTVE VTSMYASAKA WCSEKEFKAV
IPYWQSLCAK NSMELMSLAS IEPLLTDEYI NSLPQIDPEQ NNVTTTGTID SPVLLTKKYY
NRAHKSYVSH DYAMPKHKRY GWGLIGYWGA VLVLGMMSKA WTVFFSRRSV RGSCDPETRP
SLQTKKGPLT SLFHSLRTHI IMPATFAPAI PNHQQLWLSH ALPKRVDTLI VLGFWIVSII
LSCVGYDSFA GSLSVPSLYQ QNWQYTSDRT GVLAYACLPA LWLFSGRNNV FIQMTHFSVQ
SFTMFHRHIA WVCTILAVVH SINYSVLFAE YVGRYWIAWK EEYWYMGVVA TILLCFMLVQ
SMTFFQRRWY ETFLMLHIVF AVVIVVALFQ HTSFDGREWV GYLWTPVGLW VLERLARVGR
VVYCNLNARF GKQFLGTATT VTYSEASDLV KIEMVPGAAS LKPRPGQLYY IYQATLLKGW
ENHPFSLGAW APSSGANNEK SASASQNGNK LIFYVRPYDG WTRRLRDQCR KAGGTFYPKL
LLEGAYGHSE PVYAYNTLLI IVGGTGIAVA VPYLLDHIAR VKEGKTKTTK IELVWSVRQK
EMFNEVFNEE LAEIMQHNDI TITVFCTRLS KITSDSESDD VNISKEVSSG VAPVIKATGA
DSPTSNSSLR FMPGRPNIRE TVMSEVREAQ TSSTNLAVLT CGPAQMADEC RGTVYEVMKN
GFQDIEYFEE AFGW
//