ID J5QMF3_TRIAS Unreviewed; 392 AA.
AC J5QMF3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=A1Q1_02918 {ECO:0000313|EMBL:EJT48108.1};
OS Trichosporon asahii var. asahii (strain ATCC 90039 / CBS 2479 / JCM 2466 /
OS KCTC 7840 / NBRC 103889/ NCYC 2677 / UAMH 7654) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1186058 {ECO:0000313|EMBL:EJT48108.1, ECO:0000313|Proteomes:UP000002748};
RN [1] {ECO:0000313|EMBL:EJT48108.1, ECO:0000313|Proteomes:UP000002748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 90039 / CBS 2479 / JCM 2466 / KCTC 7840 / NCYC 2677 / UAMH
RC 7654 {ECO:0000313|Proteomes:UP000002748};
RX PubMed=23104369; DOI=10.1128/EC.00237-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Draft genome sequence of CBS 2479, the standard type strain of
RT Trichosporon asahii.";
RL Eukaryot. Cell 11:1415-1416(2012).
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}.
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:EJT48108.1}.
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DR EMBL; ALBS01000212; EJT48108.1; -; Genomic_DNA.
DR RefSeq; XP_014179622.1; XM_014324147.1.
DR AlphaFoldDB; J5QMF3; -.
DR GeneID; 25986431; -.
DR KEGG; tasa:A1Q1_02918; -.
DR VEuPathDB; FungiDB:A1Q1_02918; -.
DR HOGENOM; CLU_010365_7_0_1; -.
DR OrthoDB; 1776577at2759; -.
DR Proteomes; UP000002748; 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:0000041; P:transition metal 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 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 PANTHER; PTHR32361:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-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 PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..216
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 392 AA; 41391 MW; 3DE9FF5A49593C30 CRC64;
MLGVGFAPSR TSTTGGLALA ALSLLFLSSF GLFRRLAYEG FIALHILLGI VLLAALCVHR
PMYRAWAWGG FVIWGFDRIV SLGKMGWASR AGKTGKTGKT GAVVEVLGAD VVKVTVTTGM
KWTPGQHMFL TMPSIALQQH PFTMASLASA ASNASDASPA SPASDASAAS DTNAAREGGQ
AVFFIRAHKG FTRHLLSHPG PHRCLVDGPY GIPPALTHYA SVTLLAGGTG ISFCLALLLG
LVRDARRSDS AVGLVHLVWN TRDEDAVAWI KGMIEMEMGG SAGRMEVRVD VHRTRRGVET
ATPSVVSDKD EQGENDALVS VINVLEGRAD VEGTIRRNIA STPNDAGGMA VVVCGPSSLN
LETRRAVCAV NTPSAVAKGQ PPIHFYSEQF GW
//
