ID A0A0N1P2T8_9EURO Unreviewed; 666 AA.
AC A0A0N1P2T8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Ferric/cupric transmembrane component 2 {ECO:0000313|EMBL:KPI44194.1};
GN ORFNames=AB675_6643 {ECO:0000313|EMBL:KPI44194.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI44194.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI44194.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI44194.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI44194.1}.
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DR EMBL; LFJN01000004; KPI44194.1; -; Genomic_DNA.
DR RefSeq; XP_018004157.1; XM_018146948.1.
DR AlphaFoldDB; A0A0N1P2T8; -.
DR STRING; 1664694.A0A0N1P2T8; -.
DR GeneID; 28738828; -.
DR OrthoDB; 2787294at2759; -.
DR Proteomes; UP000038010; 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; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR PANTHER; PTHR32361:SF12; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14340)-RELATED; 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 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:UP000038010};
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 75..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 340..514
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 442..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 74675 MW; A26BF9DE18543B91 CRC64;
MMQHFRTPTP VSGLFRKRDF QILPGTYGSL LNSTKPPPSI ASAIANGNLT QAPNGTYYSG
LTGVNLERDR TLTRALSIAV LCLMVLVLGV RFWQVRTGRL RQIFCLTATT SQQNYWSYDR
NAWWPWLKKH IIYAPLGKVR HNREWQLSKA HNYGTTPGRV HTAILVTYII LNLVFCLYLE
YDHEIPKILA ELRGRSGMLS VFNMIALVLL ATRNNPLIWF LEISFDTFNL FHRWLGRLII
LEALAHVLAW YGAISIAKPP GGSNQAVADK PFLQYGVLGM TAFGIILVQS FSPIRHAFYE
IFLHLHQFLA FIAILGIYLH LDVADLPALP YARAVCVIWA IERLARILRL VYLNFTFKNG
VTTVVIEALP GQAVRLTFQL PRHIEVRPGS HSYVYIPRFS WHMSHPFSVA WVPSDSEPST
GMEGARYSVH PGNNIELATL PLSRPASPDS LESQSLAKEP RWMKRAKPPT SLSFVVAARS
GFTRTLYDAA SSRPYGTLEC SGLIEGPYAG HDSLGSYGTV IMFAGGAGIT HHLIQARFLL
ASAAANTVAT RKIVLVWTVR DAEQFAWVAS WMNEILAVPG RKEMLKILLY VTRGKNADYK
HKNGRLISYA GRCSPGDILD RELRDRVGAT MVSVCGPGAF ADEVRKAVRE RVDWGCLDMD
EESFTW
//