ID A0A319ELA0_ASPSB Unreviewed; 438 AA.
AC A0A319ELA0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=Aureobasidin resistance protein Aur1 {ECO:0000313|EMBL:PYI07458.1};
GN ORFNames=BO78DRAFT_89248 {ECO:0000313|EMBL:PYI07458.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI07458.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI07458.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI07458.1,
RC ECO:0000313|Proteomes:UP000248423};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KZ826341; PYI07458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319ELA0; -.
DR STRING; 1448318.A0A319ELA0; -.
DR Proteomes; UP000248423; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd03386; PAP2_Aur1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR026841; Aur1/Ipt1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR31310; -; 1.
DR PANTHER; PTHR31310:SF11; INOSITOL PHOSPHORYLCERAMIDE SYNTHASE CATALYTIC SUBUNIT AUR1; 1.
DR Pfam; PF14378; PAP2_3; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..349
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 438 AA; 49361 MW; CEA2038489ED53A3 CRC64;
MNTTLPSWKD RTQNQFGKLQ IQVPWRSIQL LVPHRMRRKI RSKLRSRLSP TSSISSLQTS
FSPVDTLRSL QSHRWTLYDF QYLLLLIIGI FSLSVMGSPG PLAKTAVFTL LLLSLLLPIT
RQFFLPFLPI AGWLIFFYAC QFVPSDWRPA IWVRVLPALE NILYGANISN ILSAHQNVVL
DVLAWLPYGI CHYGAPFVCS LIMFIFGPPG TVPLFARTFG YISMTAVLIQ LFFPCSPPWY
ENLYGLAPAD YSMPGNPAGL ARIDKLFGID LYTSGFRQSP VVFGAFPSLH AADSTLAALF
MSHVFPRLKP LFVTYTLWMW WATMYLSHHY AVDLVGGGLL ATVAFYFAKT RFLPRVQSDK
TFRWDYDYVE IGDSAREYGY DLAYDGDLNL DSDEWTVGSS SSVSSGSLSP VDDHYTWEGE
SLASPIADVE SGRHMISS
//
