ID A0A1Y2V144_9PEZI Unreviewed; 569 AA.
AC A0A1Y2V144;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ENTH domain-containing protein {ECO:0000259|PROSITE:PS50942};
GN ORFNames=M434DRAFT_23089 {ECO:0000313|EMBL:OTA90127.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA90127.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA90127.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA90127.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SIMILARITY: Belongs to the epsin family.
CC {ECO:0000256|ARBA:ARBA00010130}.
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DR EMBL; KZ112522; OTA90127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2V144; -.
DR STRING; 1001938.A0A1Y2V144; -.
DR Proteomes; UP000194361; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd16991; ENTH_Ent1_Ent2; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013182; DUF1720.
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; PF08226; DUF1720; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000194361}.
FT DOMAIN 10..143
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT REGION 159..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 63321 MW; 78B2FC86DCCD8FD6 CRC64;
MSKVMRSVKN VTKGYSSVQV KVREATSNDP WGPTGTQMSE IAQLTYNSST EFYDIVDMLD
KRLNDKGKNW RHVLKALKVL DYCLHEGSEL VVTWARKNIY IIKTLREFVY IDDDGRDVGQ
NVRVAAKELT ALILDEERLR AERSDRKTWK SRVTGIEEFG PEGVTVPAQQ RRQRPRRHSD
EDEEDAEYKL AIEASKYQEE EDRRKRESRQ GADDNDDDLA KAIKLSKEEE ERRRRELEEN
NASSLFDDDP TPSAVPQPTG MNMGYQQGSN VDWLGNPIDQ NQMMQPQPTG YMNNAYTGFP
QNGYSNGFNN GFNPQPTGIY DPYGQQQATL QAPVQQFQMQ PTGYNPYAQQ PQQFQPQPTA
SPEPVVQPGS NNPWASNSNQ NQSALKPMPT GSNNPFATGF GRPQPAKAPT MPTLSSLQAL
PEQKSLQAFS PSPQPQSQLQ PQPSFNQTQQ PQKQLSEHEQ RLNALLASGD GMDTFGNTGE
LRIPAQHTAP GTFVNSAGAG VNRLTAEATG SNPFLRQQFT GMPTVSYGSH QMPAATGPVG
MNGYGGASNP FAARPQQQNN NQGQDLIQF
//
