ID   A0A166QSJ8_9PEZI        Unreviewed;       606 AA.
AC   A0A166QSJ8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Vacuolar protein sorting-associated protein 17 {ECO:0000256|PIRNR:PIRNR011791};
GN   ORFNames=CT0861_12491 {ECO:0000313|EMBL:KZL68298.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL68298.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL68298.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL68298.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the membrane-associated retromer complex which
CC       is essential in endosome-to-Golgi retrograde transport.
CC       {ECO:0000256|PIRNR:PIRNR011791}.
CC   -!- SUBUNIT: Component of the retromer complex.
CC       {ECO:0000256|PIRNR:PIRNR011791}.
CC   -!- SIMILARITY: Belongs to the VPS17 family.
CC       {ECO:0000256|PIRNR:PIRNR011791}.
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:KZL68298.1}.
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DR   EMBL; LFIV01000124; KZL68298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166QSJ8; -.
DR   STRING; 708197.A0A166QSJ8; -.
DR   OrthoDB; 1708746at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0030904; C:retromer complex; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR   CDD; cd06891; PX_Vps17p; 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   InterPro; IPR014461; Retromer_complex_Vps17.
DR   InterPro; IPR037907; Vps17_PX.
DR   InterPro; IPR015404; Vps5_C.
DR   PANTHER; PTHR47433; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 17; 1.
DR   PANTHER; PTHR47433:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 17; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF09325; Vps5; 1.
DR   PIRSF; PIRSF011791; Vps17; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
PE   3: Inferred from homology;
KW   Protein transport {ECO:0000256|PIRNR:PIRNR011791};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR011791}.
FT   DOMAIN          136..250
FT                   /note="PX"
FT                   /evidence="ECO:0000259|SMART:SM00312"
FT   REGION          1..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..596
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  66418 MW;  5365042ADD2A8142 CRC64;
     MDYSASINDE AGASPWGSSP GSSPRPNQSN FASLGADLGG DPPGSPFRYT PSPSNAAPQD
     QENFGGEQYR RPDTASTQSA TEVETQESRT EVGSEARTSA DSPGPELPQK SQEQGGPPNP
     GGQARQDQQP RKPQQPQFRL QAKITGLERT GKKDPILRFD VHTNLPRFRT TQYRDVRRFH
     SEFVKLAEHL ISANPECLVP TVPPAVTSAG AGTDEDEARV KALLQRWFNY VCSNEVLMRD
     DEMVLFVESD FGYSPMVKMK QPATGVRRKI LKQFAPPPDD TPELQEARPI VKLFYLGTMD
     AGHKVDKLVK SRRGLGLAES DFGVKLGSMH IQEPHQGLAN AYRKLGKIVQ TVGDYHAAQA
     TAEATTIGDP FQYHSQDSFV VKESLTNRQI LIREFLQAQE NTRSKLNAAD RLKASSNVRR
     EKVDEAITAL DDARQNETYL YQKTTRVTQN LVQERRKWFA RTAADLRLSI REYVIREIEA
     ERRALAVLES VRPDIRAIDA SGGLSRLGRE SHPPVRRASV AASQGPKGDA WSGVPRRTDT
     LNRSVSGSLM AGLPEEGDGD DGQGTGQNQG LGAAGGRASL AGVAEEDDED RVDARNAASR
     LATSTF
//