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Database: UniProt
Entry: W3WLJ6_PESFW
LinkDB: W3WLJ6_PESFW
Original site: W3WLJ6_PESFW 
ID   W3WLJ6_PESFW            Unreviewed;       572 AA.
AC   W3WLJ6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN   ORFNames=PFICI_14637 {ECO:0000313|EMBL:ETS73691.1};
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS73691.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT   of natural products.";
RL   BMC Genomics 16:28-28(2015).
CC   -!- FUNCTION: Probable cell surface metalloreductase. May be involved in
CC       iron or copper homeostasis. {ECO:0000256|ARBA:ARBA00037386}.
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. AIM14
CC       subfamily. {ECO:0000256|ARBA:ARBA00038065}.
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DR   EMBL; KI912121; ETS73691.1; -; Genomic_DNA.
DR   RefSeq; XP_007841409.1; XM_007843218.1.
DR   AlphaFoldDB; W3WLJ6; -.
DR   STRING; 1229662.W3WLJ6; -.
DR   GeneID; 19279650; -.
DR   KEGG; pfy:PFICI_14637; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_005646_3_0_1; -.
DR   InParanoid; W3WLJ6; -.
DR   OMA; DENQAIH; -.
DR   OrthoDB; 367877at2759; -.
DR   Proteomes; UP000030651; 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:0006826; P:iron 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   Gene3D; 2.40.30.10; Translation factors; 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   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   PANTHER; PTHR11972:SF153; NADPH OXIDASE 4; 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   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 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:UP000030651};
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        57..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        217..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        248..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          279..404
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   572 AA;  65449 MW;  8D6A8B6A109FDADE CRC64;
     MSGYGMMDYG EKQTERSRWT PLNRILLSGE MTQERQKELT MSERFDRWMI NEGYRRFFVF
     VFMALHAMVF AFGFVNYAVK DNLQGARDTF GPTYMIARSA ALVLHIDVAL VLLPVCRTFI
     SIARQTPLNG IIQFDKNITF HITTAWSIFF FSWVHTIAHW NNFAQIAAKN NLGIYGWLLA
     NFTSGPGWTG YIMLIALTGM VITSYEKPRR ANYERFWYTH HMFIVFFLFW SFHGAFCMIQ
     PDTAPYCISV GTTAIGVFWQ YWMYGGFIYL AERVAREIRG RHKTYVSKVI QHPSNVCEIQ
     IKKENTKTRA GQYIFFCCPE VSLWQYHPFT LTSAPEEDYI SIHMRVAGDF TTAVATTLGC
     DFGKKGDKSK VVGVDAQDGD VDPALKRVLP RVYVDGPFGS ASEDVFKYEV AVLCGAGIGV
     TPFASILKSI WYRMNYPQKK TRLGKVYFFW ICRDFGSFEW FRSLLLAIEA QDVDGRIEIH
     TYLTAKIKAD DATNIMINDA NADKDTITGL RSPTNFGRPN WDMIFRGIRK LHAPAEAGVF
     FCGPKGLGSA LHIFCNKYSE PGFSFVWGKE NF
//
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