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Database: UniProt
Entry: B2W9G1_PYRTR
LinkDB: B2W9G1_PYRTR
Original site: B2W9G1_PYRTR 
ID   B2W9G1_PYRTR            Unreviewed;       633 AA.
AC   B2W9G1;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1 {ECO:0000256|ARBA:ARBA00017923};
DE   AltName: Full=Class E vacuolar protein-sorting machinery protein hse1 {ECO:0000256|ARBA:ARBA00018978};
GN   ORFNames=PTRG_06619 {ECO:0000313|EMBL:EDU49539.1};
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU49539.1, ECO:0000313|Proteomes:UP000001471};
RN   [1] {ECO:0000313|Proteomes:UP000001471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
CC   -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting
CC       receptor for ubiquitinated cargo proteins at the multivesicular body
CC       (MVB). {ECO:0000256|ARBA:ARBA00002654}.
CC   -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC       {ECO:0000256|ARBA:ARBA00011446}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the STAM family.
CC       {ECO:0000256|ARBA:ARBA00009666}.
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DR   EMBL; DS231620; EDU49539.1; -; Genomic_DNA.
DR   RefSeq; XP_001936952.1; XM_001936917.1.
DR   AlphaFoldDB; B2W9G1; -.
DR   STRING; 426418.B2W9G1; -.
DR   EnsemblFungi; EDU49539; EDU49539; PTRG_06619.
DR   GeneID; 6344882; -.
DR   eggNOG; KOG2199; Eukaryota.
DR   HOGENOM; CLU_010104_1_1_1; -.
DR   InParanoid; B2W9G1; -.
DR   OMA; VPMQAYL; -.
DR   OrthoDB; 620063at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0016197; P:endosomal transport; IEA:UniProt.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProt.
DR   GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR   CDD; cd21386; GAT_Hse1; 1.
DR   CDD; cd11805; SH3_GRB2_like_C; 1.
DR   CDD; cd16978; VHS_HSE1; 1.
DR   Gene3D; 1.20.5.1940; -; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR004152; GAT_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR002014; VHS_dom.
DR   PANTHER; PTHR45929; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR   PANTHER; PTHR45929:SF3; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR   Pfam; PF03127; GAT; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00790; VHS; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50179; VHS; 1.
PE   3: Inferred from homology;
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          16..145
FT                   /note="VHS"
FT                   /evidence="ECO:0000259|PROSITE:PS50179"
FT   DOMAIN          216..275
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          139..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..437
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..594
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   633 AA;  68574 MW;  7BD4978B0B86298C CRC64;
     MFRAQSNIFD DVVVKATDEN LTSENWEYIL DVCDKVGSSD TGAKDAVAAM IRRLAHRNAN
     VQLYTLELAN ALSQNCGIQM HKELASRSFT EALLRLANDR NTHQQVKAKI LERMGEWTDM
     FARDPDLGIM SGAYMKLKSQ NPNLRAPSKP QKTQISDVER QKEEEELQMA LAMSIRESKG
     AAPTAAKSNT PQQSGSGPSA SSEQPAKPVP SGTTAATVSR VRALFDFQPS EPGELQFRKG
     DIIAVLESVY KDWWKGSLRG QTGIFPLNYV EKLQDPTREE LEREAQNEAE VFAQIRNVEK
     LLALLSTSSQ PGAGDARDNE EITELYHSTL AIRPKLIELI GKYSQKKDDF TQLNEKFIKA
     RRDYESMLEA SMSQPQQPAY GGRPAFGGYN APPPSNYQGY PPASSTPHQD PGRFAYGGAP
     PQSGPSQVPP PGSSPAFFMV PPGEQRTQQT PKPGLPQDPY QAAMGRVPVG GRPLSYAPQE
     LATAHYDSPV DNRHSFHAPS QPQASAPPQG YDYPPSTQQA GAGYPPQQGP PQGPPHAQQN
     PYDQVTSPPL QHAPQDQQPP SDPYAQAPPQ QGYAYPPSQP AYAPPAPPGA SSSPAPPAQT
     QSYLPYRPGG AAAAPSAPSA PPVGGDDASG FYR
//
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