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Database: UniProt
Entry: G0W7V7_NAUDC
LinkDB: G0W7V7_NAUDC
Original site: G0W7V7_NAUDC 
ID   G0W7V7_NAUDC            Unreviewed;       542 AA.
AC   G0W7V7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   13-SEP-2023, entry version 48.
DE   RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=NDAI0C02080 {ECO:0000313|EMBL:CCD23868.1};
GN   OrderedLocusNames=NDAI_0C02080 {ECO:0000313|EMBL:CCD23868.1};
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:CCD23868.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD23868.1, 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; HE580269; CCD23868.1; -; Genomic_DNA.
DR   RefSeq; XP_003669111.1; XM_003669063.1.
DR   AlphaFoldDB; G0W7V7; -.
DR   STRING; 1071378.G0W7V7; -.
DR   GeneID; 11496803; -.
DR   KEGG; ndi:NDAI_0C02080; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   HOGENOM; CLU_005965_0_3_1; -.
DR   OMA; RGGIYTI; -.
DR   OrthoDB; 23943at2759; -.
DR   Proteomes; UP000000689; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10232; ScSsz1p_like_NBD; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR45639:SF32; HEAT SHOCK PROTEIN PDR13; 1.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   REGION          458..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..486
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  58814 MW;  67D65DD2ACD87CC3 CRC64;
     MSSPVIGISF GNTSSSIAYI NPKNDVDVIA NPDGERAIPS VLSYVGEDEY HGGQALQQLV
     RNPTNTIINF RDFIGLPFDQ CDISRCANSA PAVEIDGKVG FVIAKGEGKE EKLTVDEVVS
     RHLNRLKLAA EDYIGQKVNQ AVLTVPTNFT TEQKDALSTA ADKVGLKIVQ FINEPSAALL
     AHIEQFPSEK DCNVVVADFG GVRSDAAVFA IRGGIFTILA TAHDNTLGGD NLDAELIEYF
     AKDFQTKTKT NPRKNARSLA KLRINSIVTK KTLSNATTAT ISIDSLADGF DYHTSINRMR
     YELVASKVFG KFGEFINSTI KKANLDPLDI DAVLLAGGVS FSPKLATNLE YTLPESVEIL
     GPSNANASNY PNELAASGAA LQARLVADYD EDELKEALQP IIVNTLHLQK PIGLVDSEGN
     FVPILLAETS YPVQKKITLK KASGDLLIGV YEGDSTIEER TVDPAEKKAN EEADEDESEW
     SDEDDEPEVI REKKYTLSTK LMELGIKGVK SGLELVFNIN KDGKLTVSAR DLKTNQVVKG
     EL
//
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