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
//