ID G0W9B4_NAUDC Unreviewed; 486 AA.
AC G0W9B4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=ENTH domain-containing protein {ECO:0000259|PROSITE:PS50942};
GN Name=NDAI0D00610 {ECO:0000313|EMBL:CCD24375.1};
GN OrderedLocusNames=NDAI_0D00610 {ECO:0000313|EMBL:CCD24375.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD24375.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD24375.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the epsin family.
CC {ECO:0000256|ARBA:ARBA00010130}.
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DR EMBL; HE580270; CCD24375.1; -; Genomic_DNA.
DR RefSeq; XP_003669618.1; XM_003669570.1.
DR AlphaFoldDB; G0W9B4; -.
DR STRING; 1071378.G0W9B4; -.
DR GeneID; 11494929; -.
DR KEGG; ndi:NDAI_0D00610; -.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_012678_0_1_1; -.
DR OMA; STEFYDI; -.
DR OrthoDB; 1532at2759; -.
DR Proteomes; UP000000689; Chromosome 4.
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; 1.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT DOMAIN 11..142
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT REGION 143..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 56322 MW; 91B32A61F3DE5D75 CRC64;
MSKQFVRSAK NMMKGYSTTQ VLVRDATSND SSNPSFEILY EISKRSFDSV DFFEIMDMLD
KRLNDKGKYW KHIAKSLTVL DYLVRFGSEN CVLWCKQNLY IIKTLKEFKL EDDNVDESSI
IRVKAKELTA LLQDDERLKE ERSINLKNNR RSERKNRSRR GTNATRRGTK SDEDLQKALE
ESRITAEEDE RRRRELAQYD NQDTDYQTAL QLSKEEEELK KLQELQRLQQ LQQQQQQQMQ
FQQQPQQQEQ VYYDIFGNPI SPEEYLQFQQ QQQAFAQQQA LQQQHLEQQR LAEEQYRLLQ
QQQQQQQQQA YTQQQQSLQP LPTGSNNPFA LNATINTSPI RPAEQQPQPQ FTAPQQQQQP
LQQPLKQTRT GNQSISDKYN ELNNLLASGT GIDTFGNTGD QRIPAQHTQT GTFINSQGTG
YKQIVNDPVK KNPFLNNQYT GLPSSNIVPS HTGYGFGNGP QQGQGQAPPP QQQQQQSQQS
FSLIDL
//
