ID A0A1F5LNP4_9EURO Unreviewed; 434 AA.
AC A0A1F5LNP4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Inositolphosphotransferase Aur1/Ipt1 domain-containing protein {ECO:0000259|Pfam:PF14378};
GN ORFNames=PENARI_c006G04003 {ECO:0000313|EMBL:OGE54521.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE54521.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE54521.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE54521.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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:OGE54521.1}.
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DR EMBL; LXJU01000006; OGE54521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LNP4; -.
DR OrthoDB; 2097865at2759; -.
DR Proteomes; UP000177622; 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:UP000177622};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 155..212
FT /note="Inositolphosphotransferase Aur1/Ipt1"
FT /evidence="ECO:0000259|Pfam:PF14378"
FT DOMAIN 235..314
FT /note="Inositolphosphotransferase Aur1/Ipt1"
FT /evidence="ECO:0000259|Pfam:PF14378"
FT DOMAIN 340..381
FT /note="Inositolphosphotransferase Aur1/Ipt1"
FT /evidence="ECO:0000259|Pfam:PF14378"
FT REGION 48..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 48963 MW; 941332756EC76798 CRC64;
MGVGAVLEPL VVIILLFGGT WINRTTGTNA HRHFARRKSA DLVRAASPDS LESGYSSPTT
KDGLLTPRSR SPLHQIPDGW HKRQVGILGL TLEVSSPNTV IFQDRLLSRL LRKLPFLVEC
WYWALVYWTY QLGRAFTAVT LKDDTVDVAR RHALQLIKIE QRLDIFWETV IQRNFLLHPR
AMIWINWIYS FIHIPGTIAF LVWLYYFTTT RNRVDETQAG KPRGAVSGSP AGPLLYQARR
RTLAVCNLLA FVVFTLWPCM PPRLLSDTNI GGQEGELARS YGFVDTVHGT NGAGTAMPSL
HFGYSLMIGL TIMTIPLPQQ RRTVLRTRLT RVRLTLPPWR RLMCLILGFS YPFIILVAIV
ATANHFILDA VAGALVCALG WRFNGMLLNL LPLEDYFLWL VRIHKPEPSL VTVIPESLDS
RSSSEGLWSH AVIS
//