ID A0A1L7XGS7_9HELO Unreviewed; 441 AA.
AC A0A1L7XGS7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Probable aureobasidin-resistance protein {ECO:0000313|EMBL:CZR64243.1};
GN ORFNames=PAC_14141 {ECO:0000313|EMBL:CZR64243.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR64243.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR64243.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR64243.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-2016) 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; FJOG01000026; CZR64243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7XGS7; -.
DR STRING; 576137.A0A1L7XGS7; -.
DR OrthoDB; 1404225at2759; -.
DR Proteomes; UP000184330; 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:UP000184330};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..348
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 395..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 49640 MW; DB37393CE4B61F79 CRC64;
MPESKYYASS SPTTFTKAKI PFSWPSIPNP IPRRYRRRLR SKFRNAQSPA SSIARIETSF
NPADSIRALR MHRWSYYDGQ YIILIILAIF SLSISQAPGP LVKTGAASLL ILALLMPITR
QFFLPVLPIF TWLVFFFNAR FIPAEYRPHI WVKVLPALEN IFYGANLSNI LSAHQHVVLD
VLAWVPYGLL HFGGPFFWAA LMFFFGPPGT LPVFARTFGF MNIAGVAIQL IFPCSPPWYE
NMYGLAPANY SMQGSPAGLA RIDRLLGFDM YTTNFTASPL VFGAFPSLHS GNAVLEALFM
SHCFPKMRPV VIAYAMWMWW ATMYLSHHYA VDLVGGGFMA AIAFYIAKTN FLPRIQPGKF
WRWDYDYVEK GDSPIGEYEY GLTVLGNDDF RSGDSSDEWT VGSSSSISSG SRSPVDESQS
WEGETLASQT SDSELQEIIV R
//
