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Database: UniProt
Entry: J5SSX0_TRIAS
LinkDB: J5SSX0_TRIAS
Original site: J5SSX0_TRIAS 
ID   J5SSX0_TRIAS            Unreviewed;       773 AA.
AC   J5SSX0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=PX domain-containing protein {ECO:0000259|PROSITE:PS50195};
GN   ORFNames=A1Q1_03837 {ECO:0000313|EMBL:EJT47366.1};
OS   Trichosporon asahii var. asahii (strain ATCC 90039 / CBS 2479 / JCM 2466 /
OS   KCTC 7840 / NBRC 103889/ NCYC 2677 / UAMH 7654) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1186058 {ECO:0000313|EMBL:EJT47366.1, ECO:0000313|Proteomes:UP000002748};
RN   [1] {ECO:0000313|EMBL:EJT47366.1, ECO:0000313|Proteomes:UP000002748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 90039 / CBS 2479 / JCM 2466 / KCTC 7840 / NCYC 2677 / UAMH
RC   7654 {ECO:0000313|Proteomes:UP000002748};
RX   PubMed=23104369; DOI=10.1128/EC.00237-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Draft genome sequence of CBS 2479, the standard type strain of
RT   Trichosporon asahii.";
RL   Eukaryot. Cell 11:1415-1416(2012).
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004481}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
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:EJT47366.1}.
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DR   EMBL; ALBS01000256; EJT47366.1; -; Genomic_DNA.
DR   RefSeq; XP_014177737.1; XM_014322262.1.
DR   AlphaFoldDB; J5SSX0; -.
DR   GeneID; 25987350; -.
DR   KEGG; tasa:A1Q1_03837; -.
DR   VEuPathDB; FungiDB:A1Q1_03837; -.
DR   HOGENOM; CLU_014456_1_1_1; -.
DR   OrthoDB; 5475877at2759; -.
DR   Proteomes; UP000002748; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR   CDD; cd06867; PX_SNX41_42; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
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   InterPro; IPR044106; PX_Snx41/Atg20.
DR   PANTHER; PTHR46979; SORTING NEXIN-41; 1.
DR   PANTHER; PTHR46979:SF2; SORTING NEXIN-41; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT   DOMAIN          1..194
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..733
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  84024 MW;  B8B5665CCECBD3C6 CRC64;
     MEDVTNPFST SPSRSPSATP TRSPVLSRTT SHSSTNQRPS APGSVAGASS PPPTQRASFP
     DPSKEPRRGT GVLPGPKPKE GFCCERDRQI AQGEEISIID AFKTTEGGKS SYITYVIRIG
     ALQGLYPVLI IPPIPSKQSI TDYAVKGQSK TKEDVATIAT RKRLLEDFLR RVCRHPILGG
     EHVFHRFLED GSEVLHSPPI SLLPKNPLHA PSHNPTFEDV NGNDDPDSTS STSYIAHHLL
     PNPSPTHPLH RPDLRFQESE AFTDKFHQHF AHNMEKVNRR ATKRWSEHAS DMSELGAQWN
     GFSLMESGPL GTAIEKVGQA VDADFLATTK MVSYNGLLLT NPQLQDWEQN ASEPLHTYTQ
     FAQLIKSRLS FRHQKHVQYE LVQEALENQR DKLEILEAAE REARRLEQAL ERGGVAAGAS
     ASAPSSPPAR EDSSIPELAR PSVRRSGQSF GLLSAVKHSL SGMMDVDPEA TRRANIAKTR
     DNISQLEDSL QASAQDLKYA STTLQADLDR FQRQKVADLR ELTIQLSTIH RDWCKANLEA
     WKAAQAAIDE IPDHPNKVPA DAAARVASID RDRDLPPVPQ QESRRSSVAH GSPAKRDSLS
     MGGARSPSKP LSPGMGARSP SNASNPLPKM GQLNLDSPFS ETPFSSHPLG EPSAPANGLD
     PLGGSMISPR HTPKPAEDAD TPKWPSSPVK SSPPEQKSVD VPPSPKSTQA VKSLNEEARD
     EDEPVESSKG TLVDRKDSAG SVGSKLSTTN IKPADITKDT KPKTEDVGPL GPL
//
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