ID A0A068S6X6_9FUNG Unreviewed; 583 AA.
AC A0A068S6X6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Enth-domain-containing protein {ECO:0000313|EMBL:CDH57760.1};
GN ORFNames=LCOR_08665.1 {ECO:0000313|EMBL:CDH57760.1};
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:CDH57760.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH57760.1, 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:CDH57760.1}.
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DR EMBL; CBTN010000049; CDH57760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S6X6; -.
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..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..583
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 583 AA; 64534 MW; 911E9A19F68100DC 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
MQGSSSPAAD SRYAKLNSLL ANKEDGMDTF GNTGNLRVPV GSGFASSLNP QLTGAPNGNG
TSSVPSLVNV GTTDNGAQSN SFSDSFGQPS RNPFGQATSS PWK
//
