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
//