ID A0A0A2L4T0_PENIT Unreviewed; 651 AA.
AC A0A0A2L4T0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=FAD-binding 8 {ECO:0000313|EMBL:KGO74168.1};
GN ORFNames=PITC_022260 {ECO:0000313|EMBL:KGO74168.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO74168.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO74168.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO74168.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO74168.1}.
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DR EMBL; JQGA01000705; KGO74168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L4T0; -.
DR STRING; 40296.A0A0A2L4T0; -.
DR HOGENOM; CLU_016134_0_0_1; -.
DR OMA; LYSGILW; -.
DR OrthoDB; 1759852at2759; -.
DR PhylomeDB; A0A0A2L4T0; -.
DR Proteomes; UP000030104; 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:SF3; REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13750)-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:UP000030104};
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 54..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 315..447
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 651 AA; 72583 MW; 2FD039C682C99631 CRC64;
MSSPKLDVRH IQNLSAATSL EPHWGYYDRA LPCTNDPGSC EYLDLVYASH DRGMLYSGIL
WCVIGTFLLL WVVLNQFNTQ RMSPALATPE LAGLHKVRRS VVSLARKYLL PDAARFIFGR
TTRLQVLTLA VLAGYLLIFS FVGIIYKKWV TPVSKMPGVY NTRSSIGPWS DRIGTLAYAL
TPLSVLLSSR ESFLSLITGL PYQSFNFLHR WLGYIIFAQS SLHTISWCVV ELRMYQPQPT
VGLEWVTQTY IVWGIVAMIL LLLLVVLSTP WGIRLTGYET FRKLHYILAM VYIGACWAHW
KQLKCFMWPS LIFWFLDRGA RLVRTALLHY HPDHSGTLGL GFKPADATIT RFPDTEHGDV
IRLDLHNNQD PWSIGQHYYL SFTKCSIWQS HPFTPLNLPT VSKGTVQHSY ILRAKSGETK
NVADLAATGT PTTPVILTGA YGESITNHLT PSTNIICVAG GTGITYVLPV LLDLARQQPS
PDRKVELIWA VRHTANTEWI AAELDLLQKA RNMLNLEIRI FATRDSGSKT PSIENSDSGN
CNLAVPKIGE KVVQVSPSKS VSTCCGCDKP TAVERLGDAS DDVSRHPDLP RLVDDFLAQT
VRGPTSVFAS GPGGMISDLR DIVASCNSGV KVWKGQERFD VGLICDDRLE W
//
