ID A0A371DDV4_9APHY Unreviewed; 511 AA.
AC A0A371DDV4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=ENTH-domain-containing protein {ECO:0000313|EMBL:RDX50721.1};
GN ORFNames=OH76DRAFT_1402342 {ECO:0000313|EMBL:RDX50721.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX50721.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX50721.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX50721.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
CC -!- SIMILARITY: Belongs to the epsin family.
CC {ECO:0000256|ARBA:ARBA00010130}.
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DR EMBL; KZ857398; RDX50721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DDV4; -.
DR STRING; 139420.A0A371DDV4; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0051179; P:localization; IEA:UniProt.
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 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; 2.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT DOMAIN 14..146
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT REGION 136..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 58383 MW; 66CE236F8551954E CRC64;
MQHLGKGIVR GVKNYTKGYS DVQAKVREAT SNDPWGPSGT QMNELAQLSY NQDHFVEIME
MLDKRLNDKG KNWRHVFKSL TVLDYLLHAG SENVVVYFRD NIYIIKTLKE FQYVDEEGKD
QGANVRQKAK DITNLLQDES RLRHERRDRA MMRDRMVRGR GEDGDDNENE RRRSQSVPGG
GRRRNGTNRE DDDLRKALEE SKRTAEEEQA RLRMTAEERD IQQAIRLSEE EEAKRAKAVQ
DANQSALFDD AQQPQPTGTN PFPLVDTSFQ GQPQFLQPQF TAVPQQFTSF NPYQQQAQQE
AMQAEYMRQQ QEWQMQQQLQ AQQQQQQQQE EWMRQQQLLQ LQQQQQQQQQ FLMPQQPLVP
QATGFGSNNP FAPSLAMSTP SLPTQLSSPG PQTTSPVSFN LQGTYGQGPT STAPPPVSHS
APPEAPRANS VPAVKTRADD EHAHLANLLA NREDGIDTFG NWGNLRYGQQ ASRLINEPTG
SQRGNHNPFA QQQQQQQQHQ QQSSDQPFFS I
//
