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Database: UniProt
Entry: A0A1V6S4I9_9EURO
LinkDB: A0A1V6S4I9_9EURO
Original site: A0A1V6S4I9_9EURO 
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
//
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