ID J7RGP0_KAZNA Unreviewed; 646 AA.
AC J7RGP0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=ENTH domain-containing protein {ECO:0000259|PROSITE:PS50942};
GN Name=KNAG0B02650 {ECO:0000313|EMBL:CCK68708.1};
GN OrderedLocusNames=KNAG_0B02650 {ECO:0000313|EMBL:CCK68708.1};
OS Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK68708.1, ECO:0000313|Proteomes:UP000006310};
RN [1] {ECO:0000313|EMBL:CCK68708.1, ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
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).
RN [2] {ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Kazachstania naganishii.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the epsin family.
CC {ECO:0000256|ARBA:ARBA00010130}.
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DR EMBL; HE978315; CCK68708.1; -; Genomic_DNA.
DR AlphaFoldDB; J7RGP0; -.
DR STRING; 1071383.J7RGP0; -.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_012678_0_1_1; -.
DR OMA; HTGFVQP; -.
DR OrthoDB; 1532at2759; -.
DR Proteomes; UP000006310; Chromosome 2.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000006310}.
FT DOMAIN 11..144
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT REGION 141..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..390
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 156..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 73901 MW; 39202CD63EE44A8B CRC64;
MSRQFVRSAK NVMKGYSSTQ VLVRDATAND GRTPHLDTLE DIAGLSFDSV DFFEIMDVLE
KRLNDSGKYW RHIEKSLTVL DYLVRFGSEH CADWARDHLF LLKALRNFRF VDDGIGFDQG
QIVRVKARDL VELLQSGEQL GGRKAKRARG ASRRDRGRRR GGDRGGGEYR QRGDDPEDEY
YPRPAGGPPP QRQGYESGGA RGNDDDDLQR AIEESKRTVQ EDEERRRQLS MYDEEDPEFQ
AALQLSREEE ELKNLQHLQR LQQQQQQQQQ QQQLNTAYLD VFGNPVSQDE YQEYQRQQQV
WEQQQEQQRL AQDQYMQLQQ QQQAQEQALQ QQQQQAQEQA LQLQQQQQAQ EQALQQQQQQ
QQALQQQQAQ EQAMQQQQQQ QQQFLQAQQQ QPMTTGSNNP FAVNAAPIQQ PNYTQSPNNY
VSPQQNYAPP QPPRPSQPSQ QQSPQQSPQQ AYNPYSSPQQ VPNAQFSGNV PTGSPGQEAH
GRAPAPVPQP MPRMNTGNQE VTNKYSELNN LLAQGTGVDT FGNEGTQRIP AQHTQTGTFI
NSQGTGFKQV NSEGKDPNSN PFLNSQYTGL PSTGIVPAYT GYGFGNQSDQ QNAPQQQQQY
QQQPQQQQQQ QQQPQQQYQQ QPQQPYQQQP QQQQQPPDQV VSLIDL
//
