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Database: UniProt
Entry: A0A0S7E5F4_9EURO
LinkDB: A0A0S7E5F4_9EURO
Original site: A0A0S7E5F4_9EURO 
ID   A0A0S7E5F4_9EURO        Unreviewed;      1216 AA.
AC   A0A0S7E5F4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Intermediate filament protein {ECO:0000313|EMBL:GIM43006.1};
GN   ORFNames=ALT_002620 {ECO:0000313|EMBL:GIM43006.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM43006.1};
RN   [1] {ECO:0000313|EMBL:GIM43006.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM43006.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC       {ECO:0000256|ARBA:ARBA00010883}.
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:GIM43006.1}.
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DR   EMBL; BCLY01000016; GIM43006.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7E5F4; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_8532; -.
DR   OrthoDB; 5392990at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   CDD; cd06876; PX_MDM1p; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR013937; Sorting_nexin_C.
DR   PANTHER; PTHR22775; SORTING NEXIN; 1.
DR   PANTHER; PTHR22775:SF3; SORTING NEXIN-13; 1.
DR   Pfam; PF08628; Nexin_C; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF02194; PXA; 1.
DR   Pfam; PF00615; RGS; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00313; PXA; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS51207; PXA; 1.
DR   PROSITE; PS50132; RGS; 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        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        32..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          564..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..637
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1216 AA;  136029 MW;  462F1C9E18107783 CRC64;
     MALNRRDIIL FSTGGFIAWG LVVRWLPILR YLGYALVLGA LLSCTALLTA VFLTIRPLDS
     AKPPRPSSLP LAFLLPKHWP REVEGIRARS TYRADSLYPQ SFIVSESIDE LLSLVTRDFI
     ASWYQHISPN PAFVNEVDRV IRAAIGNLCN RLLAEDLISL VVSRIFPILT AHLKEFDVAE
     KSVRGRNLTR NVTESEELDL AIAKKYRDGR LHPAAALSVS EQKVVEQEYL RKITLGLLPK
     LFPEHVLNSR IVTVLIREIL ACAVLFPLVS VLSDPDTWNQ LVEAYGRTTI QDRKTVQKIR
     AALDEHASPA PKTKRGHPFP KLAPNDSERA FERFVRAIRR CNNLSDARRF RALVASQLKR
     ESMVEGQDPV YLRRLETGKR VLDQKVAKLS APGGNNTPYA NAVESHFRRN SSSSKPEASL
     VDVMHDASGL SYFMEFMDRQ KLMSLVQFWI VVDGFRNPLE DDFGDETSPS SSTWTTADRN
     DMALISETYL AKPELKVSEE ARRAVKAFLN AGKRATPEQY RKARTVILST QSAVLEELQA
     VYYPKFKQSD LYYKYLASDE VSVAGSRASP APVESPARRP LPPLMARTAS HPGQKPKDLR
     RAVASSSDVR SMGKLFDDEE ETRRSIDSER SAPLFDDDYD TDPLAASTHS LGTDSQSGFN
     DATQKQAIKS MEAALNDIIT NDPGNANLGD VKYIDSGSAG SFSVDRGLKS PRSTGDLGRL
     DNRTDDNKAK PNIASLGLVD QSSRIGVFDD ELFPDQQKFL EDEYDEPPET DDKDPADEVQ
     EAAPGDLGLT EAIEALTADI EKLAAQEAVI DALTRKADLT NNTAELRILR KSKASIQREI
     HRKEMQRQQY IIQESDNSLY GRSTVRIQSI VVGKEEDGRE YAMYVIEVQR NAGEQMPAAS
     WAVARRYSEF HELHQRLRMS YPSVRHLEFP RRRMVMKLQK EFLQKRRLAL EAYLRNLLLL
     PEVCRSRDLR AFLSQRAIIP RDETPRDGET KDLVTRIYNS VADGMDDFLG NFGVLDQLSA
     AGQNLISAAT NHQNSLVSNS GLATEDAVTA AEAEAELNAF EDRELEPFIK PICDLFLEAF
     ELNKGNNWLR GRAVVVVLHQ LLGGTIERKV REGARSLVQD ESLLRYLSMA KETMWPGGVL
     RQNKVRTASE RLKSRTEASL VLATLIPDVA GNVVGRANAQ GAARRIFATL NNQRLNSHLI
     FSILDEVVLV LFGGAK
//
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