ID A0A319DF94_9EURO Unreviewed; 1224 AA.
AC A0A319DF94;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Intermediate filament protein {ECO:0000313|EMBL:PYH95864.1};
GN ORFNames=BO71DRAFT_376690 {ECO:0000313|EMBL:PYH95864.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH95864.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH95864.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH95864.1,
RC ECO:0000313|Proteomes:UP000247810};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; KZ825847; PYH95864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319DF94; -.
DR STRING; 1448320.A0A319DF94; -.
DR Proteomes; UP000247810; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000247810};
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 DOMAIN 101..290
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 418..555
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 863..981
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 303..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1224 AA; 137416 MW; AD51B6BA0234B294 CRC64;
MTLKRREFVL LGTGGFIAWG LVVQWLPVLR YLGYALVLGA FVSSAILIGL VLLTIRSPND
PASLSSKTLH VAFLAPSHWG KEAQSYRSRS IYHPKSLYPQ SFVVSKGIDE LLTLATRDFI
ASWYQYISPN PAFVNEVDRV IRTAVGNLCD RLLAEDLVSL LVSRIFPILT AHLKEFDVAE
RLVRGRNLTR NVTESEELDL AIAGKYREGH LHPAAVLSVS DQKLVEQEYL RKIAVGLLPQ
LFPESVLNSR IVSVLVREIL ACAVFFPLVS ALSDPDTWNQ LVEAYGRTAI QDRKTVRKLR
AALDEHASPA PRPKRGHSFP RLSPHDSERA FERFVRAIRR CNNISEARRF RALVTSQLKR
EMMVEGQDQV YLRRLETGKR VLDQKVAKLS APGGTQLSHA SAAVTHFRRK NSVPQEASLV
DVMHDASGLS YFMEFMDRQQ LMSLVQFWIV VDGFRNPLED DFGDESSASS TTWTPADRSD
MALISETYLS KSELKVTDES RRVVKAFLGA GKRATPEQYR RARTVILSAQ SAVLEELQEN
YYPKFKQSDI YYKYLASDDV LHSGTQSPHH GSPNTFEVPE RRPLPPLMAR TSSQPGSKSK
DLRRAAVSSS DVRSMGKLFD DDESSRHSFD SERSAPLFDD DYDTDPLAMS TQSLSRDSQN
GETEVNQNEV IENMEAALND IIANEPKNSR IEDLKSADIP STGPPSTNQS PKSPRSSVEF
SRAENRAEDR MKPSIASLGL VDRSSRLGVF DDDLFPDQHK FIEDEYDEPM GMDNDPDDHV
HEAAPGDLGL TEAIEVLSAD IEKLGSQESV VDTLTRKAEL TNNTAELRIL RKSKASIQRE
IHRKEMQRQQ YIIQESDNSL YGRSTVRIKS IVVGKEEDGR EFAMYVAEVQ RNAGEQMPAA
SWVVARRYSE FHELHHKLRM RYPSVRHLEF PRRRVVLKLQ KEFLQKRRLA LEAYLQKLLL
LPEVCRSRDL RAFLSQRAII PRNEAQSSNN GETKDLVTRI YNSVADGMDD FLGNFGVLDQ
LSTAGQNLIS AATNQQASTV PDSGIATEDA VTAAEAEAEL NAFEDRELEP FIKPICDLFL
ETFELNKGNN WLRGRAVVVV LHQLLGGTIE RKVREGARSL VQDDSILRYL TLAKDTMWPG
GVIRQSKVRT ASERLKSRTE ASLVLATLLP DLAGNVVGRA NAQAAARRMF ATLNNRRLNA
HLAFTIVDEI VLVLFGGGEA GRMR
//
