ID A0A0U1LRZ7_TALIS Unreviewed; 440 AA.
AC A0A0U1LRZ7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Inositol phosphorylceramide synthase catalytic subunit aur1 {ECO:0000313|EMBL:CRG85271.1};
GN ORFNames=PISL3812_02377 {ECO:0000313|EMBL:CRG85271.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG85271.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG85271.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG85271.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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; CVMT01000002; CRG85271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1LRZ7; -.
DR STRING; 28573.A0A0U1LRZ7; -.
DR OMA; WSIYDAQ; -.
DR OrthoDB; 1404225at2759; -.
DR Proteomes; UP000054383; 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:UP000054383};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 82..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..351
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 396..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 49375 MW; 2090173606E73B08 CRC64;
MMSPSISIPT WKDRQQTQFG KIPVMPWRSF KLLMPHRMRR RLRSRLRSRQ SPASSIASMQ
TSFSPRDTLR SLQSYRWSAY DFQYLLLMII GIFSLSIIQA PGPVGKTAIA SLLLTSLLLP
ITRQFFLPFL PIAAWLIFFY ACQFVPSEMR PGIWVRVLPA LENILYGANI SNILSAHQNT
VLDVLAWIPY GLCHYGAPFV VSIIMFIFGP PGTVPVFAKT LGYISLTAVA IQLIFPCSPP
WYENRFGLAP ADYSMQGDPA GLARIDALLG IDLYTSGFHA SPVVFGAFPS LHAADSTLAA
LFMSHVFPKL KPLFVTYTLW MWWATMYLSH HYAVDLVTGG ILAAVAFYFA KARFLPRIQR
DKKFRWDYDY IERGNGPDED GYDLAHLDGD VSLDSDEWTV GSSSSISSGS LSPTEDQHLW
EGETLASYSD IEARPLGNKL
//
