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Database: UniProt
Entry: A0A5C3M5K5_9AGAR
LinkDB: A0A5C3M5K5_9AGAR
Original site: A0A5C3M5K5_9AGAR 
ID   A0A5C3M5K5_9AGAR        Unreviewed;       955 AA.
AC   A0A5C3M5K5;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=ANTH domain-containing protein {ECO:0000313|EMBL:TFK39925.1};
GN   ORFNames=BDQ12DRAFT_649527 {ECO:0000313|EMBL:TFK39925.1};
OS   Crucibulum laeve.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Nidulariaceae; Crucibulum.
OX   NCBI_TaxID=68775 {ECO:0000313|EMBL:TFK39925.1, ECO:0000313|Proteomes:UP000308652};
RN   [1] {ECO:0000313|EMBL:TFK39925.1, ECO:0000313|Proteomes:UP000308652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 166.37 {ECO:0000313|EMBL:TFK39925.1,
RC   ECO:0000313|Proteomes:UP000308652};
RX   PubMed=30886374; DOI=.1038/s41559-019-0834-1;
RA   Varga T., Krizsan K., Foldi C., Dima B., Sanchez-Garcia M.,
RA   Sanchez-Ramirez S., Szollosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA   Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA   Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA   Damon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA   Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA   LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA   Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA   Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA   Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA   Grigoriev I.V., Vagvolgyi C., Papp T., Martin F.M., Miettinen O.,
RA   Hibbett D.S., Nagy L.G.;
RT   "Megaphylogeny resolves global patterns of mushroom evolution.";
RL   Nat. Ecol. Evol. 3:668-678(2019).
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DR   EMBL; ML213598; TFK39925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C3M5K5; -.
DR   STRING; 68775.A0A5C3M5K5; -.
DR   Proteomes; UP000308652; 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   Reference proteome {ECO:0000313|Proteomes:UP000308652}.
FT   DOMAIN          1..126
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   REGION          140..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..869
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        901..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   955 AA;  101385 MW;  1EDAA058BFEFEBAE CRC64;
     MSSFDKVVKL ACKPKAAPPK AKYLDPIIAA TWSDDGAVHD VCKALSPRFR EPNHIVVFKA
     LIVLHTMIRN GATDNVLSYL SQSDVLKLRN VSSGNWEGYA APENLQNYSV YLDSRIRAYR
     DLKHDAVRVQ AESNRDMRNS ISIEEDGYKS RKDQGGKPAS TGPTRSKTIM GRKLRVMTVE
     KGLLRETKAV HRMIDALVEC RFYLDDLEDE LTITALRMLV KDLLILFQAG NEGVINVLEH
     YFEMSQVDAQ EALVIYRHFC KQTERVVEFL GVAKKLQNLL NVPIPNLKHA PVSLAGALQE
     YLEDPNFEQN RIEYKANKDA AERVTKKSAD PKSKKSESSG SKPTTSASTS TATQGASNGS
     TSTGLKENKD IIDFFTAIEE EQPSMFNPQT NSPSSAYFQQ QAANPFAQMT TSQPFAVQVA
     PQQTGFLMPQ QTAFQAPNPF NLIAQQQQQM QPQPTGHRPF SSFIQPQQTA FQQQPQQSFQ
     QPQQTGIQQQ QPQQGFQQQP QQNSFLRPQP TGFLQPQATG SNPFRQSMLM PQSTGMALFG
     GMGPQGGSSP FPGQNQPQQS QGSFGLQGQN PSGPMTAPGA SFSSQPASPF AQMPSNTPTN
     VPARPASTPL TAFGPSSASG ASPPMAQPVK THQTGTKNPF GPIATAPPPV PKPPTLMELS
     LGGANNGWQA GQQQQQQQQQ QQPQATGSFG NGFGFSSSAL SPGATDISSI ASSFATGNKT
     NTTSNDNQQS GTSGFSLSGP LGSQNTTTTT TTGSTFSDSL FSSSPLSTQP TGFTNTPSSP
     SIAVSPPLKP QFTGFSGLKA FKPSSSFGTS LLESLPPIPG STPTTPAING STPAGGANPS
     SGFSSTFNSQ NTGFGALNSQ STGATGGFGG GSTLGQGLRP QMTGGGGANP FRASMMGIST
     PPPMPSFNGN TTPSSMPGFM GGMSSQSFAT NVGGPKFGSN PNPNHGGQQQ GSSLI
//
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