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Database: UniProt
Entry: A0A139IMA2_9PEZI
LinkDB: A0A139IMA2_9PEZI
Original site: A0A139IMA2_9PEZI 
ID   A0A139IMA2_9PEZI        Unreviewed;       592 AA.
AC   A0A139IMA2;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Sorting nexin-4 {ECO:0000256|ARBA:ARBA00040748};
DE   AltName: Full=Autophagy-related protein 24 {ECO:0000256|ARBA:ARBA00041273};
GN   ORFNames=AC579_1419 {ECO:0000313|EMBL:KXT15918.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT15918.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT15918.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT15918.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-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:KXT15918.1}.
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DR   EMBL; LFZO01000047; KXT15918.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139IMA2; -.
DR   STRING; 113226.A0A139IMA2; -.
DR   Proteomes; UP000073492; 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:UP000073492}.
FT   DOMAIN          186..307
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          42..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          508..535
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        150..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   592 AA;  65908 MW;  6AB34C663142CF55 CRC64;
     MTDQAHLGET SRGVHGSGSE ASQLQIGEHE LQHVWQQHNV DNNTSTTTTL STSPADHESV
     RSHSSPAHSI TIELSPPVPA QDELSDVDSD FDIIGGSQLI PEASYDGIAS SNEGIFHGWA
     AKIPQGLRRS SKQPERRISG DWPELPGTGT MDAGSSSSND YNSPEWQQAG EHADPQDLAG
     PGAHGRLECK VSSPQKEGEG TQNPYVSYLV TTHTDFKSFM QSHIQVRRRY TDFVFLYRTL
     SKEYPQCAVP PLPDKHNMSY VRGDRFGPDF TNRRAYSLNR FLKRLTLHPV MRRATLLALF
     LESSDWNATM KSRPNRGMSG SESGSGSVLE SWTDSFLNAF TKPHKTDKRF QDVNDRASKL
     DDDLGTVSKT VARVAKREGD LEADYGDLAT QFQKLAALEP GVNDELTKFA TSVHSTSEGW
     KDLKDFTDQD YLGSLKDMEA YITAVKALLK TREQKQLDFE GLTEYLNKAA QERDTLASHG
     SIGASGFLRQ KIEDVRGVDH EQARRERQRK LEVQISRLTT EVEAAKKTTE AFDEEVVKEV
     ADFERIKAVE FRDTLGGLAD ANIKFFQNNI EIWERFVQDM EKGQAAAAKA SG
//
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