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Database: UniProt
Entry: F4NYN5_BATDJ
LinkDB: F4NYN5_BATDJ
Original site: F4NYN5_BATDJ 
ID   F4NYN5_BATDJ            Unreviewed;       737 AA.
AC   F4NYN5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN   ORFNames=BATDEDRAFT_87228 {ECO:0000313|EMBL:EGF81738.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF81738.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF81738.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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; GL882881; EGF81738.1; -; Genomic_DNA.
DR   RefSeq; XP_006677511.1; XM_006677448.1.
DR   AlphaFoldDB; F4NYN5; -.
DR   STRING; 684364.F4NYN5; -.
DR   GeneID; 18242719; -.
DR   HOGENOM; CLU_372527_0_0_1; -.
DR   InParanoid; F4NYN5; -.
DR   OMA; WTHELVA; -.
DR   OrthoDB; 367877at2759; -.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR   GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR   GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
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   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972:SF69; METALLOREDUCTASE AIM14-RELATED; 1.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 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:UP000007241};
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        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        569..588
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        623..644
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          340..450
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   737 AA;  82686 MW;  857CC20728D1C5A6 CRC64;
     MGVIAASPRK PILSPTVVRL AARILATLAM LVALVASYAL ASMVEGGKLR WSSSIMVVDR
     FDQWILGFAL LPMFIATLST FFSDPNTPDS IVTGRNDEYT ISADGRSSTA HSTPLHCSGF
     WNPRFKFLGK YSTLFKPWSQ GDIMITCLLV ISNILWWIAP VITRLYLKPS KTLSTPRGML
     ARFAIWAAMA GLWNAAMAIV FVVRENHITK NIVGKDAGQF HRGLRYHIAL GYTSFVQITF
     HGTYYLTIMV IDGAFPNEIL PTLSDTGYSN FFGFLAWLSL MLMALTSIFK VRRANYRIFY
     WTHQLYTCFL LFAFMHQTRT WYPVMASLVY FIFDRLLPRL KTQRTTSALL TRVSPSVVRL
     DIAILQTYAD SCTYSPGSWV NILVPSISHF NWHPFSISSS HHLTPRTVTL YIKARGAWTT
     QLHASSTGLG VMVPIKMDGF FGSRNNSYLS YQHLVVVGAG TGIATIIPYI YSYAQHTLGK
     ITVFWLARTA VEACAYRSLL EALSDPNSPL AGRVDLHLHL TREQDSRVST KHDHRIGSGF
     NGNPNFASTL SKSVGYEQSS TTTKPSYRLS AIFLSIIVFS AAAVGYVIGR TYVPAYNADE
     CNADEAYTLV GLSHFMCWYY PQWAPTGFAC LFAAISGLAF VWMVSLMKQT DAAVSNVEPI
     DVTPASFEWF KERFTWVAHR PNFAYELESV FNFYNSIENQ SNIKIAVIAG GPERMVRDIE
     NVVIDHGQAF FRESWKM
//
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