ID A0A318ZJT0_9EURO Unreviewed; 445 AA.
AC A0A318ZJT0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Inositolphosphotransferase Aur1/Ipt1 domain-containing protein {ECO:0000259|Pfam:PF14378};
GN ORFNames=BP01DRAFT_293386 {ECO:0000313|EMBL:PYH46634.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH46634.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH46634.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH46634.1,
RC ECO:0000313|Proteomes:UP000248349};
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 (DEC-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; KZ821227; PYH46634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318ZJT0; -.
DR OrthoDB; 2097865at2759; -.
DR Proteomes; UP000248349; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd03386; PAP2_Aur1_like; 1.
DR InterPro; IPR026841; Aur1/Ipt1.
DR PANTHER; PTHR31310; -; 1.
DR PANTHER; PTHR31310:SF7; PA-PHOSPHATASE RELATED-FAMILY PROTEIN DDB_G0268928; 1.
DR Pfam; PF14378; PAP2_3; 3.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 156..212
FT /note="Inositolphosphotransferase Aur1/Ipt1"
FT /evidence="ECO:0000259|Pfam:PF14378"
FT DOMAIN 236..327
FT /note="Inositolphosphotransferase Aur1/Ipt1"
FT /evidence="ECO:0000259|Pfam:PF14378"
FT DOMAIN 354..394
FT /note="Inositolphosphotransferase Aur1/Ipt1"
FT /evidence="ECO:0000259|Pfam:PF14378"
FT REGION 27..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 49730 MW; 1F330A112BFAEB7D CRC64;
MGAGAILEPL TVIVLLFGGT WINRSTGKFP PRRPHRNSNV SRGSSPGAVE SGLSTPTAKD
TLLNRRSSSS SSLQQVGQAG WRKRQIGFFA STFEVTSPDT TVFHDRLLSR LLRKFPFLVE
CWYWALVYWT YQLGRAFTAV TLKEDTVDVA RKHALQLIQI EQALGMFWEV SIQKYFLRHP
TLMTWTNWIY SFIHIPGTIA FLVWLYYFTI TRNRSDESQP GKPRGLVGGS PAGSHLYQAR
RRTLAVCNLL AFVVFTLWPC MPPRLLSDKD AKGPDAALGR SYGFVDTVHG VNGAGSVWTE
NRFCNQYAAM PSLHFGYSLM IGLTIMTIPL PPHQRRRTRV AIGPLKLQLP SWRRLGCLVL
GFAYPFVILA AIVATANHFI LDAIAGATVC ALGWRFNGIL LNLLPLEDYF LWLVRIHKPA
PNTMDGLADA VGWVDDGVPE HTSLP
//
