GenomeNet

Database: UniProt
Entry: A0A319A8I4_ASPLB
LinkDB: A0A319A8I4_ASPLB
Original site: A0A319A8I4_ASPLB 
ID   A0A319A8I4_ASPLB        Unreviewed;      1024 AA.
AC   A0A319A8I4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   RecName: Full=PXA domain-containing protein {ECO:0000259|PROSITE:PS51207};
GN   ORFNames=BO96DRAFT_466584 {ECO:0000313|EMBL:PYH56207.1};
OS   Aspergillus lacticoffeatus (strain CBS 101883).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH56207.1, ECO:0000313|Proteomes:UP000247441};
RN   [1] {ECO:0000313|EMBL:PYH56207.1, ECO:0000313|Proteomes:UP000247441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH56207.1,
RC   ECO:0000313|Proteomes:UP000247441};
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   -!- SIMILARITY: Belongs to the sorting nexin family.
CC       {ECO:0000256|ARBA:ARBA00010883}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KZ821351; PYH56207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319A8I4; -.
DR   OrthoDB; 2727031at2759; -.
DR   Proteomes; UP000247441; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   CDD; cd06093; PX_domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR013937; Sorting_nexin_C.
DR   PANTHER; PTHR22775:SF47; MEIOTICALLY UP-REGULATED GENE 122 PROTEIN; 1.
DR   PANTHER; PTHR22775; SORTING NEXIN; 1.
DR   Pfam; PF08628; Nexin_C; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF02194; PXA; 1.
DR   SMART; SM00313; PXA; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS51207; PXA; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        88..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..372
FT                   /note="PXA"
FT                   /evidence="ECO:0000259|PROSITE:PS51207"
FT   REGION          396..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          713..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..769
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..793
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..848
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1024 AA;  112597 MW;  985C160E6A671E43 CRC64;
     MSSRETQIKM NIFADHIYTL RVPIAMDETS NWAEQSQPKK PELAETPHIV LPTSYNEQAV
     TESSNSVRSK GAIDSTLQFL STSNGETLLG VFACLVGATL LLFGRLGLLL IGIASGIILH
     AQWEAADEDP TQPLSNSRHR RRKELALDIA RRLLDWPKST DSAADAGQDD IGQVFLFGDT
     SSADLEYSTL GPKTAAALRS ITDAIMRDYV ISWSSPILPP ETTFPLSCRK LLAEFISSLS
     SHLSRKRSAD TFLELLTNSS SLIIVFLDEL SAAFESVGSN EPPEEVVLRY MESSPESGLA
     NILAKDQQKR KLDIIADDIL ARFLDPNVYG CLLLKDFMRE MFVSVLFEST ISSLSRPEII
     NGWIIYLFNE GKSEIMTAID AGVEGAQEQV VTATRDLNSV NEPSSETTSN TSPEPNITGD
     EIQQETADVD RATVEAKIEA KRLSDMITAH DMQKQSLERA IRDDVQEVAL DDRIDHGEDL
     PANKIGDDIM QREDSGCDQA KHIGVNIDFK LEENNSSSPL LMPSKSQTAP NSPPEPVVLH
     RASITVETDA SKVTSKGPLR SKPTSDYLLQ VEPVSTRSTG WMVFRKYTDF ESLHQTLEAI
     SRLHKIRTFA DDHPVVPPWK GQTRSELAKN LGRYLQDALS HRSMAESERM KRFLGKDEHL
     GSDFSNPYSK TVFPFPSQSA LENVGKGVLG VLSNAPRGVS GSGKAMLDGM TGVFGGGSSK
     KQSPDPVAGD KDRSLDLFNQ SESIGHGSQE KIGDSTRTRP ASPPDRSLTR KTSGKPGHPP
     EENFPDRIET ATDYPEFSDS SVQTTDAGRT VASTQPSPSA GRYTSADLRQ SPGGTQDNFH
     TNSEGQAPDA ELSDYRSRSN PITHEETRIA VELIFAVINQ LYTLSSAWNI RRTLLNAAKS
     YILRPGNPHL ETIRELLQVS MIDSHTSDEA IGLYLNKLRE SALPTESELE NWPPPSTDTE
     KERLRETARK VFVQRGLPQA LTSVMGANAS KEVLGKIFDC LQVQNLARGF VYSLFLQALK
     AAIL
//
DBGET integrated database retrieval system