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Database: UniProt
Entry: A0A2G4SZQ4_RHIZD
LinkDB: A0A2G4SZQ4_RHIZD
Original site: A0A2G4SZQ4_RHIZD 
ID   A0A2G4SZQ4_RHIZD        Unreviewed;       281 AA.
AC   A0A2G4SZQ4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=ANTH-domain-containing protein {ECO:0000313|EMBL:PHZ14249.1};
GN   ORFNames=RHIMIDRAFT_278617 {ECO:0000313|EMBL:PHZ14249.1};
OS   Rhizopus microsporus ATCC 52813.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ14249.1, ECO:0000313|Proteomes:UP000242254};
RN   [1] {ECO:0000313|EMBL:PHZ14249.1, ECO:0000313|Proteomes:UP000242254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ14249.1,
RC   ECO:0000313|Proteomes:UP000242254};
RX   PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA   Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA   Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT   "Lipid metabolic changes in an early divergent fungus govern the
RT   establishment of a mutualistic symbiosis with endobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00243}.
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DR   EMBL; KZ303846; PHZ14249.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4SZQ4; -.
DR   STRING; 1340429.A0A2G4SZQ4; -.
DR   OrthoDB; 1424668at2759; -.
DR   Proteomes; UP000242254; Unassembled WGS sequence.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|PROSITE-ProRule:PRU00243};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242254};
KW   Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00243};
KW   Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00243}.
FT   TRANSMEM        257..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00243"
FT   DOMAIN          1..123
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
SQ   SEQUENCE   281 AA;  32372 MW;  25994AD2DD0150C2 CRC64;
     METAIRKATR LDYNPPKQKH LSTLVSLTYE NPGNAVYIVD LLERRLRENS WIIIFKVLII
     LHTLMRNGDG DKTIAYIETK PSALDTTKLR EKSSGVVHIQ NIYLYTAYLQ QKVIAYRQSK
     IDYIKDTMGK KEGRLRHLSI SDGLLKETVS IQKLIGTLLK CNFLLDDVDN NISLYAFRLL
     VEDLLVLFQV LNEAIVNILE HYFAMKKSDA RTSLEIYKRF ARQTEETISF LDRARRLQHE
     LSISIPSVKH VTIIINLYHS LLIFARIGAI IFGSSFTRVL G
//
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