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Database: UniProt
Entry: A0A367YLE3_9ASCO
LinkDB: A0A367YLE3_9ASCO
Original site: A0A367YLE3_9ASCO 
ID   A0A367YLE3_9ASCO        Unreviewed;       539 AA.
AC   A0A367YLE3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN   Name=AIM14_0 {ECO:0000313|EMBL:RCK66695.1};
GN   ORFNames=Cantr_03334 {ECO:0000313|EMBL:RCK66695.1};
OS   Candida viswanathii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK66695.1, ECO:0000313|Proteomes:UP000253472};
RN   [1] {ECO:0000313|EMBL:RCK66695.1, ECO:0000313|Proteomes:UP000253472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK66695.1,
RC   ECO:0000313|Proteomes:UP000253472};
RA   Ahn J.;
RT   "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT   Korea University).";
RL   Submitted (JUN-2018) 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}.
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:RCK66695.1}.
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DR   EMBL; QLNQ01000001; RCK66695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367YLE3; -.
DR   STRING; 5486.A0A367YLE3; -.
DR   Proteomes; UP000253472; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
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; 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; SFLDF00463; AIM14; 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.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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:UP000253472};
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:ARBA00022448}.
FT   TRANSMEM        23..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        68..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        138..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        201..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          101..216
FT                   /note="Ferric oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01794"
FT   DOMAIN          249..325
FT                   /note="FAD-binding 8"
FT                   /evidence="ECO:0000259|Pfam:PF08022"
FT   DOMAIN          353..523
FT                   /note="Ferric reductase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF08030"
SQ   SEQUENCE   539 AA;  62057 MW;  F891C5145D86068E CRC64;
     MSNTSPQSIE PRHGGHHNAN VKYGFIIFAI SIVHILFFLQ AKFIQVYRWK SRGRFSKTLS
     TFNSPPTWLV MVLWFLIVFF VGGHKITEFL EEYITIAKRY GRIAYCLLPL NIYLVLRPTN
     SAYLKPGYYL ENLSLHKWIS RLIAFCTLIH AIGFVYKWSK EGTLLEKPFR FLNFLGVLVF
     VMFAVLIVIS VRFLRRKYYS VFYIIHNVTA WLMVVLIVFH ARPGVTTFGV ICLVLLGYQL
     YLRFYAAYRV NTFKVIDIPT STLEIVKVPK PANFPPWLPG SHIRLNYGIS NVRSWVGATH
     PFTIANIPED GVNYLTLIVK KTNNFVIDQY LSYLLTGPYV SIVPPFFNTA KIINIICGGS
     GISFGLPVLN HYRSLNLHIP VRLVWCVRNQ SDTFIMNQID MTGVQVYITS AGEDASADEP
     LSSSSYQPVP LFVIDEEQQE QPAKAPEDDQ DEVNGLLDEE GIPLQNIKKE TDNEKEQPKN
     VFKYGRPKFD EVFAFDDPTL TPDYNDSWVI ACGPDQLIKD AKRWSKEKDY RFYSEKYEM
//
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