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Database: UniProt
Entry: A0A5B1QHX1_9AGAM
LinkDB: A0A5B1QHX1_9AGAM
Original site: A0A5B1QHX1_9AGAM 
ID   A0A5B1QHX1_9AGAM        Unreviewed;       943 AA.
AC   A0A5B1QHX1;
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:KAA1469092.1};
GN   ORFNames=DENSPDRAFT_557678 {ECO:0000313|EMBL:KAA1469092.1};
OS   Dentipellis sp. KUC8613.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Hericiaceae; Dentipellis.
OX   NCBI_TaxID=1883078 {ECO:0000313|EMBL:KAA1469092.1, ECO:0000313|Proteomes:UP000322482};
RN   [1] {ECO:0000313|EMBL:KAA1469092.1, ECO:0000313|Proteomes:UP000322482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8613 {ECO:0000313|EMBL:KAA1469092.1,
RC   ECO:0000313|Proteomes:UP000322482};
RX   PubMed=31482283; DOI=.1007/s00253-019-10089-6;
RA   Park H., Min B., Jang Y., Kim J., Lipzen A., Sharma A., Andreopoulos B.,
RA   Johnson J., Riley R., Spatafora J.W., Henrissat B., Kim K.H.,
RA   Grigoriev I.V., Kim J.J., Choi I.G.;
RT   "Comprehensive genomic and transcriptomic analysis of polycyclic aromatic
RT   hydrocarbon degradation by a mycoremediation fungus, Dentipellis sp.
RT   KUC8613.";
RL   Appl. Microbiol. Biotechnol. 103:8145-8155(2019).
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:KAA1469092.1}.
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DR   EMBL; NSJX01000005; KAA1469092.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5B1QHX1; -.
DR   InParanoid; A0A5B1QHX1; -.
DR   Proteomes; UP000322482; 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:UP000322482}.
FT   DOMAIN          1..126
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   REGION          133..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          884..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..588
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..943
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   943 AA;  99054 MW;  7CD29117E61494DF CRC64;
     MSSFEKVVKN ACKPKAAPPK SKYLDPIVAA TWSEDGAVHD VCKALSPRFR EPNAIVVFKA
     LIVLHTMIRN GATDNVLSYL SGSEVLRLKN VYGGQWEGYK APQNLQNYAM YLDSRIRGYR
     ELKHDAIRVQ SESNRDARLS MSLEEDARRS GRSKPESRPA GAPQRSKTVM GRKLRVMTVE
     KGLLRETKAV HKMIDALVEC RFYMDDLEDE LSLTALRMLV KDLLILFQAG NEGVINVLEH
     YFEMSHVDAE QALAIYRHFC KQTEHVVEYL GVAKKLQNLL NVPIPNMKHA PVSLVGALEE
     YLNDPNFEQN RIEYKTNKEA AERSAKSGKP AKKEEAPPLP KPATEAPAAS SSTDAPKPEG
     GKALSDFFSA IEEEQQTMFN PQTNSPTANY FQQQAAHNPF VQRQMTGGFQ SQPFGQPQIQ
     FQNTGFIQPQ MTAVPFQQQQ QPQSFSAFLQ PQTTGFLQPQ ATGSNPFRQS TLMPQTTGLS
     PFGPANPLQP TPTGSLNPFP TNPQGQFPSG QASAPSTQSA FNHVPTFNAF QPSPNVPNFA
     AASQASNTGF SAPARPSSTP ITAITARTSS PPLQPVKSHQ TGSRNPFGAP QPSAPPPMPK
     APTLMELAMG GGSIQNQQQQ QQQPMQTQQT GINGFGNSGS PSQPQGSVMA NVASAFSFNK
     PDAGSGNNSS PTTSGISSFT PNGTTASPLT NQMTSTTTSG STFSDSIFSA LSGQPTGATS
     TNSAFQSSSS PPLKPQTTGF SGMKAFKPTS SFGATLLESL PPIPQSAPTT PAASNHASPA
     PSGASSPNPT AGLPSFSTGL GNTFGQSSVS GPGSGAGLGL SSQMTGLPAL NGQQTGAGGM
     AFGGGSTVGV GLRPQMTGAG GANPFRATMF STSPGPGLPF GGAGTGALGS SNSTPAFGGQ
     GVGGGGPLFP QSTGAGLFSG AYGQQQQQQG AQQGQQQNGA SLI
//
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