ID A0A068S929_9FUNG Unreviewed; 588 AA.
AC A0A068S929;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Enth-domain-containing protein {ECO:0000313|EMBL:CDH57761.1};
GN ORFNames=LCOR_08665.1 {ECO:0000313|EMBL:CDH57761.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH57761.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH57761.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the epsin family.
CC {ECO:0000256|ARBA:ARBA00010130}.
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:CDH57761.1}.
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DR EMBL; CBTN010000049; CDH57761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S929; -.
DR STRING; 1263082.A0A068S929; -.
DR VEuPathDB; FungiDB:LCOR_08665.1; -.
DR OrthoDB; 1532at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR CDD; cd16991; ENTH_Ent1_Ent2; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR12276; EPSIN/ENT-RELATED; 1.
DR PANTHER; PTHR12276:SF110; FI19443P1; 1.
DR Pfam; PF01417; ENTH; 1.
DR Pfam; PF02809; UIM; 2.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00726; UIM; 2.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50330; UIM; 1.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586}.
FT DOMAIN 12..144
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT REGION 156..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 65059 MW; E4D0C306DDBEF311 CRC64;
MTGKGVVRSI KNYAKGFSDV QRKVREATSN DPWGPSGTLM NEIAQLTYNQ HDFIEIMDMI
DKRLNDKGKN WRHVFKALLL LDYCIHVGSE NVVLYAKENI YVIKTLKEFQ HVDDNGRDVG
ANVRQKAKDI TSLLLDDARL KDERRQRQQM RERMAGVNDY MNDAMGIRNP DMAGGRPSYG
PSNEDRELQR ALEESKRMAD DEERKRLGRQ EDEDLQKAIR LSEQEAQDKE RKQREKLERE
NQEKLFGSNN QSSSFNPFPA NQSFDSSLNP YQQQQQWPQN TGMTNMTFSD PISANNQQLG
FQNTGMTSNP YQQQQQQSNP YQQFPGFGQN LQAQMTGMPQ QMTGMAPFQT STMTGFQQPQ
MTGFQQPQMT GFQQSQMTGF PQQQQQQQPS MSTVSSSPMA SFQQPQITAA SNNPFGPLNN
QQQQPQSTGM FGQSLTASPS LASSSLAPRS PSMSVANTTT TTNSSSAAGQ SRSFTFPSPS
MQHTGTQGSS SPAADSRYAK LNSLLANKED GMDTFGNTGN LRVPVGSGFA SSLNPQLTGA
PNGNGTSSVP SLVNVGTTDN GAQSNSFSDS FGQPSRNPFG QATSSPWK
//
