ID A0A094AZV9_9PEZI Unreviewed; 1036 AA.
AC A0A094AZV9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=F-box domain-containing protein {ECO:0000259|PROSITE:PS50181};
GN ORFNames=V490_00110 {ECO:0000313|EMBL:KFY03642.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFY03642.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFY03642.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFY03642.1,
RC ECO:0000313|Proteomes:UP000029320};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY03642.1}.
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DR EMBL; JPJS01000043; KFY03642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094AZV9; -.
DR STRING; 1437433.A0A094AZV9; -.
DR HOGENOM; CLU_282867_0_0_1; -.
DR Proteomes; UP000029320; 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; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
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 PANTHER; PTHR32361:SF26; FAD-BINDING 8 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR PROSITE; PS50181; FBOX; 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:UP000029320};
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 6..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 593..638
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 526..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 115236 MW; 89B17989A578ECC1 CRC64;
MDAIQIYAIA AGGTLCIFAF VNLLPLLVPL VTHVSNFVSK HFRYPYILHR HRILGPWTRA
GVVIQLAYLA INLFCVFVIL SWDGLKAANF SDAGRRAGTL AEVNMIPLLA GPHFAFLADL
IGLSLKTIRG VHRSAGWMTA ALVFLHAMAA ASDGPFPIDV SQNLFAVVGA SLLCLILVLL
LPLFRKLSYE LFLRSHQALA LAFIYAVWRH VPSDKSFPRA YIYYDRTKPS PGAPSMPCGD
TFLPTSLPRA PISISLWGYS QQHTSCKLAP SSSETGSFAT NYHAPLSRTM QYINLWIPSV
SFWSFLQTHP FTVISWDAKD QVKLDLLIEP RRGLTRELLY HAKKGYTINP LVMFSGPHGA
NLSMGEYESV LMVASGFGIA AFVPHLKKLI YGYNTRAVRT RRIHLVWQIK SEADGLAVQE
VLNSALKEDK LDDGCILSIS VYVESKSSPK TPFGERASMY PGPAPLPEIF LAELSGNNIK
VHAAEVGAEG QKVLESTLQG DVESGSRWTV AGDGRMLVAA SREDPPRRIL PGARTSKEYA
PGSSLLRGQC SSETLSPKRT PLGELDSSSS TLPAIDHSRP FNVSTMTFDN PELTPLEMLP
TEILQAVIGH LVPWNIKRLS CTSKRLRQAS LSILFRHVKF EFSLAGMKGL KELLKSNVCG
HISSFTYIIT ELLKTEILDF DLFKSDIVTP DMYMEYAQDM YDEGYEPDEF QSYMAIYKTV
HDICSEQRSI IDEGADLILS SIFCALPLLR EVRLSFREVL EVDDWPASDM IIKEELYRHH
LQVVSSAIQS ARSVGVAIHT VSLSNFNLPY HHRWEQPNLD PLSESLRQLL GDIKVLRVCG
VDDSVLELLS HCVPDLQQLD MCQVYAPEKV IKEFFETNKT SIRSIGFHEI NIPGLSYLDS
FTPLSASMLC RCAAQQRGYN GCATTASAIA QRLSQPMWGK AVPGLPHVFC RASRADPTVL
AHMHIRVNPR RVPDMVNDTA YATKAWTSCS QVVLANPDTS TDSSLQYFEV PWTVTVRLHI
KRQPPRPLNK ASIIRL
//
