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Database: UniProt
Entry: R7YQ84_CONA1
LinkDB: R7YQ84_CONA1
Original site: R7YQ84_CONA1 
ID   R7YQ84_CONA1            Unreviewed;       586 AA.
AC   R7YQ84;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE            EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN   ORFNames=W97_03209 {ECO:0000313|EMBL:EON63979.1};
OS   Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Coniosporium.
OX   NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON63979.1, ECO:0000313|Proteomes:UP000016924};
RN   [1] {ECO:0000313|Proteomes:UP000016924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Coniosporium apollinis CBS 100218.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-
CC         siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342,
CC         Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000496};
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}.
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DR   EMBL; JH767566; EON63979.1; -; Genomic_DNA.
DR   RefSeq; XP_007779296.1; XM_007781106.1.
DR   AlphaFoldDB; R7YQ84; -.
DR   STRING; 1168221.R7YQ84; -.
DR   GeneID; 19900520; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_010365_7_2_1; -.
DR   OMA; IDETHEP; -.
DR   OrthoDB; 1776577at2759; -.
DR   Proteomes; UP000016924; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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; PTHR32361:SF23; FERRIC-CHELATE REDUCTASE-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   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:UP000016924};
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        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        73..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        141..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          197..315
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   586 AA;  64638 MW;  7A4A70C231242650 CRC64;
     MALVVFSTVV SCILSFAQRP WYRDHLGQTP LGSRTGFMAA AMMPLIIALA AKVNIITIIT
     GIGHEKLNAL HRWLSWIFLA LSLIHTIAFL IQPLREGGRP RLHEALYKHA SFLYSGVPPL
     AFLVAIMALS FPIIRRAAYE FFAWSHVTMS VIFLGLLFWH FANLYDSWHY LWATMAVWLF
     SLLGRAFHKI SFFRLSSSWL RGCPAAVHSI SPDMLKMEIL APPGWSWEPG QHVFLRFPQF
     NLFDNHPFTI ASIPNRSSTP RTPLGVPTQS SQNTLEFLIR PQSGFTRRLL HYTDEHPDAL
     LSAVIEGPYG TALPRLENRY EDVILVAGGA GITAMLPWLL HIAERMRAGG CATRRVRLVW
     ITRSKGDVNW IGGQLRRMWE VAPGGSVGVD VWATRKPLRE VARVKTVKEA FGTIASGPAQ
     PSLASPLSLS PVSPRAPLSL TSPLGLSPVS PKTPGLGTPM LPWTPTGLAP PVSLRFPASP
     VSPVSPVDSM FSGRSGGSGK RLLKGIRETV RDAGSPLDDF VEMHVGARPD IERVVGVMIG
     DRRTAVLGCG PEGLKIDLSN LVAREQKRVI RGQAKEVMLH TETFDF
//
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