ID A0A0F7VD76_PENBI Unreviewed; 397 AA.
AC A0A0F7VD76;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Putative Arsenical-resistance protein {ECO:0000313|EMBL:CEO58616.1};
GN ORFNames=PMG11_03327 {ECO:0000313|EMBL:CEO58616.1};
OS Penicillium brasilianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=104259 {ECO:0000313|EMBL:CEO58616.1, ECO:0000313|Proteomes:UP000042958};
RN [1] {ECO:0000313|Proteomes:UP000042958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG11 {ECO:0000313|Proteomes:UP000042958};
RX PubMed=26337871; DOI=10.1128/genomea.00724-15;
RA Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Brakhage A.A.,
RA Valiante V.;
RT "Draft genome sequence of the fungus Penicillium brasilianum MG11.";
RL Genome Announc. 3:0-0(2015).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|PIRNR:PIRNR005508}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|PIRNR:PIRNR005508}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59)
CC family. {ECO:0000256|ARBA:ARBA00010110, ECO:0000256|PIRNR:PIRNR005508}.
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DR EMBL; CDHK01000003; CEO58616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7VD76; -.
DR STRING; 104259.A0A0F7VD76; -.
DR OrthoDB; 5482285at2759; -.
DR Proteomes; UP000042958; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015103; F:inorganic anion transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR004706; Arsenical-R_Acr3.
DR InterPro; IPR002657; BilAc:Na_symport/Acr3.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR NCBIfam; TIGR00832; acr3; 1.
DR PANTHER; PTHR43057:SF1; ARSENICAL-RESISTANCE PROTEIN 3; 1.
DR PANTHER; PTHR43057; ARSENITE EFFLUX TRANSPORTER; 1.
DR Pfam; PF01758; SBF; 1.
DR PIRSF; PIRSF005508; Acr3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR005508};
KW Membrane {ECO:0000256|PIRNR:PIRNR005508, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000042958};
KW Transmembrane {ECO:0000256|PIRNR:PIRNR005508, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR005508,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR005508}.
FT TRANSMEM 64..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 43379 MW; 5A688FD78546D6F2 CRC64;
MTSPKSSTHS LPTATAEPQS LSTTVTKDRP NFTGGDVEKQ RTNENEEPPS QQSAFKGLGW
LDRFLAIWIF LAMVIGILLG NFVENTGPAL QKGKFVGVSI PIAIGLLVMM YPILCKVRYE
SLHHVFNERA IWIQIAFSIF VNWIIAPFLM LGLAWAFLPD EPELREGLIL VGLARCIAMV
LIWTGLAGGD NEYCAILVAI NSILQMVLFA PLAVFFINVI SHSGSQVTFS YSTAAKSVAV
FLGIPLGAAI ITRMTLRKIT SPRWYDQVFV KCISPLSLLG LLFTILVLFA SQGRQVVHQI
VSVIRVSAPL IVYFIIVFFI TLLVTYKLGF GYKLAATQSF TAASNNFELA IAVSVATFGA
DSNQALASTV GPLIEVPVLL GLVYVAKFIG KRLGWKD
//
