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Database: UniProt
Entry: G0WFY8_NAUDC
LinkDB: G0WFY8_NAUDC
Original site: G0WFY8_NAUDC 
ID   G0WFY8_NAUDC            Unreviewed;       455 AA.
AC   G0WFY8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Zinc finger PHD-type domain-containing protein {ECO:0000259|SMART:SM00249};
GN   Name=NDAI0I01300 {ECO:0000313|EMBL:CCD26699.1};
GN   OrderedLocusNames=NDAI_0I01300 {ECO:0000313|EMBL:CCD26699.1};
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:CCD26699.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD26699.1, 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).
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DR   EMBL; HE580275; CCD26699.1; -; Genomic_DNA.
DR   RefSeq; XP_003671942.1; XM_003671894.1.
DR   AlphaFoldDB; G0WFY8; -.
DR   STRING; 1071378.G0WFY8; -.
DR   GeneID; 11493553; -.
DR   KEGG; ndi:NDAI_0I01300; -.
DR   eggNOG; KOG1844; Eukaryota.
DR   HOGENOM; CLU_020879_1_0_1; -.
DR   OMA; PEKYWCE; -.
DR   OrthoDB; 5491784at2759; -.
DR   Proteomes; UP000000689; Chromosome 9.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15550; PHD_MLL5; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR47793; HISTONE DEACETYLASE COMPLEX SUBUNIT CTI6; 1.
DR   PANTHER; PTHR47793:SF1; HISTONE DEACETYLASE COMPLEX SUBUNIT CTI6; 1.
DR   Pfam; PF20826; PHD_5; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          54..103
FT                   /note="Zinc finger PHD-type"
FT                   /evidence="ECO:0000259|SMART:SM00249"
FT   REGION          112..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          24..51
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        120..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  52205 MW;  0A5E08B8B29C58E4 CRC64;
     MSVVTKEFQT QPGNEDPKQL AVAAAVAEEE VKEEEEDIAD VDVEAEEEEE EITRCICGKI
     DLPDGDSGLY IQCEQCSVWQ HGYCVGILEN DNVPDKYWCE LCKPELHQIA PSGKSSIYKG
     SKEIEPKEQE EVQEDTRKID DDAYDNLVAE GENDDEHNKK LQRNNNDHVD ALHTDDQKED
     VDDDMIPDKP DHEPTPETTK QIRDNRKRAT TMEREEKQYQ LMLQKAIDAS KLVGNPEDDN
     ATKESKNEHD EMKDEEEKLN GEEKDNIKNN ETTNFKNDSN SSSFTNSTKK SISPPASLTS
     EETDVKEEIM KKPAPRRSTR VTKPRINKSR SNTSVNSNTS TTKRNAARKL KDNNSNNTYN
     DNDIALSKSV KPRIPPKRTT MNEMRRRSAA ILEYISRTQW ELSGEQASRD QIARFVDNDK
     FIKEKIDSIY DKHNDLLKSM DELAKQVIHW EEKYC
//
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