ID   A0A0D1YVS0_9EURO        Unreviewed;      1387 AA.
AC   A0A0D1YVS0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Autophagy-related protein 26 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV11_06537 {ECO:0000313|EMBL:KIV78938.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV78938.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV78938.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV78938.1,
RC   ECO:0000313|Proteomes:UP000053599};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN846953; KIV78938.1; -; Genomic_DNA.
DR   STRING; 1016849.A0A0D1YVS0; -.
DR   HOGENOM; CLU_001720_0_0_1; -.
DR   OrthoDB; 2027807at2759; -.
DR   Proteomes; UP000053599; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   CDD; cd07609; BAR_SIP3_fungi; 1.
DR   CDD; cd13280; PH_SIP3; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR039463; Sip3/Lam1_BAR.
DR   InterPro; IPR042067; Sip3_PH.
DR   InterPro; IPR031968; VASt.
DR   PANTHER; PTHR14248; CYCLIN Y, ISOFORM A; 1.
DR   PANTHER; PTHR14248:SF18; CYCLIN Y, ISOFORM A; 1.
DR   Pfam; PF16746; BAR_3; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF16016; VASt; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51778; VAST; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          311..412
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          951..1122
FT                   /note="VASt"
FT                   /evidence="ECO:0000259|PROSITE:PS51778"
FT   REGION          291..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          880..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..676
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1387 AA;  154655 MW;  08C7C8F4100EDF6E CRC64;
     MSETLQPAND VGRLINLVPV GLKEAAIDSP TSRATVVHYG EQVELLEKWL DDYFKATNRL
     VAESLTLENV LNSFISHSVL PLTISESMLD HDYSTLAMKK YGEGAKDYWM SAVGVVKKLT
     TMVSDPIRQF MTNDLRAFKD VRRAVEASQK TFEHLQSKYA GLGKSKEPSS LREDAFQLHE
     ARKTYLHAMM DFYSLIPQFR FALDRLLVQI FFEQWKEMRV SRDNTAATVQ RSAGEMQRVR
     GWLNEMEASE RTFRKELLTA KKQLEEAAEL STRPSRELDD YSLSTIPQFS SHAHTTGGMS
     QSSPKKVAPR TGEKQGWLFL RTYGGKPTRT IWVHRWAFIR NGVFGWLLQS ARAGGVEESE
     RIGVLLCNVR PAPAEERRFC FELKTNKNTI LLQAETQAEL VEWIGAFESA KSKALEDPNA
     TQNLSGGGNI QTGAAFAISA PPIPEFGTYV LGSTEPGTAG DDIAALEKSN TLPVPGSEAA
     RESSVDLPRR STAAEEGGHR DTASRIISKL DLHRKSAASP LVSPTPSTPN LPAGGIASLI
     AASHGSMPVG PAIPMVQNPE LDVRPRHTFT LALRDMPPST LAPATLAAVP SPTNLSKAAV
     IVTGERGLSP APYKSGIPTS LIANLWGTSN TALVNRLERS EPKTHPEIKL ATQPSPVFKT
     SPSPPNPSPS PPRRPGMPHT AVSQLDLSIP QNFTRSRTPS PSKRHRSTIS VDRDAFRHIK
     SDLLVSEFPN YYPLQLKSQD AQFRLLFPDV RRDERLVMVF RATWNPNEQQ EFPGRVYVTS
     KDLYFYSNHM GLVLTTSLPL GSIDEATAAP GRDCDFVFLH LTEPGSDGSN RRITLKTFLE
     PLKLLQKRLN FLIKNSVSQE PLELEELIKA LLKMESESGD RSPSLESWED VSPNTPVDTG
     GLRYRDRAST IGTEVRAPLR VDRALHQTQL GRRESKFKLP AQPVKYVPTG NLRLATEKEF
     DISAKALFHV MFGDKTAIWQ LLQHERRAKN LNQGPWLSLG EGRLRREFAF DIPTTTILGQ
     GAWAHVRDYQ VVDVNSDHLC YVVTDKRTPW HLPFQDRYRL VSKIVITHVA KAKCKLALFI
     KLEWTSSAGI LGGMLERQAL YDLEFDCLDL ADLVADQVRK LGAHSRTKKA VQIFGQVGHA
     SETTQLIVND SAFAIELRRP PFQTTITGLL SRRAASASQS AVAMALASLI DFVKWMNKTL
     SANKFILVAL LLSALYNSWH TYRDSLGWWH ERRASKFMAR LGVSPDVVMS RAVYLNDLDE
     VLHYDASMPV GDSSACYSVF SDAHDPEVIH AGAGNSGNAQ FQQTRQRLGV YRHDLLVAVR
     VVNGIEKELM QSAWEQWVVD ENRRCNVVEG LVLNDGAHNA TDVSEDVKSW YDEYCVSCRE
     EYNKIKI
//