ID A0A2S4KP82_9HYPO Unreviewed; 459 AA.
AC A0A2S4KP82;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=Inositol phosphorylceramide synthase catalytic subunit aur1 {ECO:0000313|EMBL:POR32017.1};
GN ORFNames=TPAR_07761 {ECO:0000313|EMBL:POR32017.1};
OS Tolypocladium paradoxum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=94208 {ECO:0000313|EMBL:POR32017.1, ECO:0000313|Proteomes:UP000237481};
RN [1] {ECO:0000313|EMBL:POR32017.1, ECO:0000313|Proteomes:UP000237481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRBC 100945 {ECO:0000313|EMBL:POR32017.1,
RC ECO:0000313|Proteomes:UP000237481};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:POR32017.1}.
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DR EMBL; PKSG01000927; POR32017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4KP82; -.
DR STRING; 94208.A0A2S4KP82; -.
DR OrthoDB; 1404225at2759; -.
DR Proteomes; UP000237481; 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:UP000237481};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..173
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 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..324
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 459 AA; 51249 MW; C7B6D3F68965206B CRC64;
MKDLAGSVPG KPVLPSLWTE NLTLAVLSRL PSRYQVGRRR ARAKSGSTRP DVPDITSLET
SFNFWDGIRD LQRHKWHVVD LQYIFLAGLT LFSLSIAPSA PALKLFALVG GVWLMLMPAT
RQFFLPSATI WVWLVYFFCS RFIPYEYRPR IWVRVLPALE NVLYGANLSN ILSAHTHAVL
DILAWLPYGI IHFGAPAVCS LLIFIFAAPG TTPVFARAFG WMSILGVTIQ LVFPCTPPWY
ENEHGLVPAA YGMPGSPAGL ARVDKIFGID LYTTNFTAAP LPFGAFPSLH GGYAVLEVLF
MSHCFPQFRI FFIGYAAWIW WATMYLSHHY AIDLVGGGLI AMAFYYTARS RWLPRRQADK
ITRWDYEYVE TGDRHRIGDE EYGDQCFSLG LLEHRRGNSS DGWTLGSGSS YSSSSGTVSP
TASEGPSGML LVDMENNGRL WDGSAPPRDV ELSEVVVLR
//
