ID A0A0F4GT41_9PEZI Unreviewed; 587 AA.
AC A0A0F4GT41;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Sorting nexin-4 {ECO:0000256|ARBA:ARBA00040748};
DE AltName: Full=Autophagy-related protein 24 {ECO:0000256|ARBA:ARBA00041273};
GN ORFNames=TI39_contig339g00041 {ECO:0000313|EMBL:KJY00208.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY00208.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJY00208.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJY00208.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KJY00208.1}.
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DR EMBL; LAFY01000331; KJY00208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GT41; -.
DR STRING; 1047168.A0A0F4GT41; -.
DR OrthoDB; 51972at2759; -.
DR Proteomes; UP000033647; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR CDD; cd07628; BAR_Atg24p; 1.
DR CDD; cd06863; PX_Atg24p; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR45949; SORTING NEXIN-4; 1.
DR PANTHER; PTHR45949:SF2; SORTING NEXIN-4; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT DOMAIN 179..300
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 501..528
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 65366 MW; 5161E6BC3EE45DA8 CRC64;
MPGSRGKKER SAKTDQSRDN DDYSRIGLSR HENGHVSSRL DTPPTALAST RRMSQERGTS
PASSTHSSIE YILTAPPSDD PDIDSDPDSD FDFCGDEAAQ PTASNGANNL QGNHYSNPPA
ELSNKQLAQK FSAFNTLYGS GSSMEAGSSN SDFGGQQDWE QAGHDATEQD LAGPGHHGRL
ECTVSQPQKE GEGTQNTYVS YLVTANTDFK SFQSSHITTR RRFTDFVFLY RTLQKEYPQC
AVPPLPDKHN MSYVRGDRFG PDFTARRAHS LGRFLTRLTL HPVLRRATIL VLFLESNDWN
ATMKSRPQRG MSGSDGGNSS VLESWTDGFL NAFTKPHRPD QRFQDVNARA SKLDSDLGTV
SKTVARVAKR ESDLEGDYAD LATQFQKLAA LEPGVEDELT RFAASVQTTS EGWKGLKDHT
DQDYLGSLKD MEAYILSVKS LLKTREQKQL DFEGLTDYLT KAAQERDTLA SHGSMGASGF
LRQKIEDVRG VDHEQSRRER QRKLEVQISR LTTEVENAKK TSEAFDEEVV KEIADFERIK
ASEFRDTLGS LADAHVGFFE NNIKIWERFV EEEEGRQKEI DAAAKAG
//
