ID   G3ASM3_SPAPN            Unreviewed;       677 AA.
AC   G3ASM3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=ENTH domain-containing protein {ECO:0000259|PROSITE:PS50942};
GN   ORFNames=SPAPADRAFT_142685 {ECO:0000313|EMBL:EGW30709.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW30709.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL996504; EGW30709.1; -; Genomic_DNA.
DR   RefSeq; XP_007376742.1; XM_007376680.1.
DR   AlphaFoldDB; G3ASM3; -.
DR   STRING; 619300.G3ASM3; -.
DR   GeneID; 18870474; -.
DR   KEGG; spaa:SPAPADRAFT_142685; -.
DR   eggNOG; KOG0251; Eukaryota.
DR   HOGENOM; CLU_014248_1_0_1; -.
DR   InParanoid; G3ASM3; -.
DR   OMA; SSTHMLH; -.
DR   OrthoDB; 1424668at2759; -.
DR   Proteomes; UP000000709; Unassembled WGS sequence.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:InterPro.
DR   GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR   CDD; cd16988; ANTH_N_YAP180; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 1.20.58.150; ANTH domain; 1.
DR   InterPro; IPR011417; ANTH_dom.
DR   InterPro; IPR014712; ANTH_dom_sf.
DR   InterPro; IPR045192; AP180-like.
DR   InterPro; IPR013809; ENTH.
DR   InterPro; IPR008942; ENTH_VHS.
DR   PANTHER; PTHR22951; CLATHRIN ASSEMBLY PROTEIN; 1.
DR   PANTHER; PTHR22951:SF89; PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN LAP; 1.
DR   Pfam; PF07651; ANTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF89009; GAT-like domain; 1.
DR   PROSITE; PS50942; ENTH; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000709}.
FT   DOMAIN          1..133
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   REGION          423..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          352..423
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        423..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   677 AA;  76996 MW;  9254378C16C533B1 CRC64;
     MTTYEKIVKG ATKVKVAAPK PKYIEPILMA TSIEHSVGSE NFNTIMRTLH LRLQDSSWSV
     VYKALIVIHI MIREGDRDVT LKYLSHKAQN MLNLSQTSLS MNSSFSSDVR FIMKYSKYLL
     TRVKQYEATG IDYVRDERSN NSTNQQGGRL RTLSIDKGLL REVESVQKQI DALLKNNFME
     SEINNDIVLT AFRMLVNDLL ALFQELNEGV INILEHYFEI SKVDAERSFK IYKKFVDQTK
     YVIDYLRVAK HLEYATKLHV PTIKHAPTAL TSSLEEYLND PNFEANRRQY LAEKSNKPVD
     PPKKQHFSLS PEQQDTVKQI DNKHQSLIVQ QSTYNPWGAI FGDNTQPSQV QQDQAQVQLQ
     QQQAQLQQQQ QQQQAQQQVQ QQALEQQAQQ QQLALQQQQL QQQQLQQQQL QQQQLALQQQ
     QQQPHIIQHS NPTGFSPLPA IVQGQPFQAP QSPPTYNGGY VPQPQQPQPL QRQNTNPFMQ
     QPVVQQITQQ QIQPVQQIQA FPGLARSNTN PFATRSVTQP IQPLQPQSTN PFGNTRFASG
     SGTTAFTNGS QTQQQSPLKA SSTGSNPFKV SSTTQNLFDN ASTQQQQPQQ IKPQATAGGL
     ELLPTIPVFP ETQKEAQKQQ YMQNAFTGIQ AQMQQQQQQG FPQQVFPQQQ QAFPQQGFPQ
     QFGVQPQYTN YDGPSLI
//