ID   D2VPY3_NAEGR            Unreviewed;       540 AA.
AC   D2VPY3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC41085.1};
GN   ORFNames=NAEGRDRAFT_71097 {ECO:0000313|EMBL:EFC41085.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC41085.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC41085.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; GG738888; EFC41085.1; -; Genomic_DNA.
DR   RefSeq; XP_002673829.1; XM_002673783.1.
DR   AlphaFoldDB; D2VPY3; -.
DR   STRING; 5762.D2VPY3; -.
DR   EnsemblProtists; EFC41085; EFC41085; NAEGRDRAFT_71097.
DR   GeneID; 8855955; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_71097; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   InParanoid; D2VPY3; -.
DR   OrthoDB; 3125219at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
SQ   SEQUENCE   540 AA;  62150 MW;  A1922AC702615CB1 CRC64;
     MNAPCCLHVG NSHATLVSST LKESSRNRFR LFDYKLLEED EAIILLSLSL SDEFDDEKIG
     REIQPSDDDL NPHRLVTNIA NLIINGKQQR DDNHIYSPYR ALQFMNSREE EIEIEIGNGI
     TVSPLDLYLK IMKTMLERNC ANMKNRLAIA VPDYFPYAVY QLIRKKVSEW GYNVMNVYSE
     SRLSLIAYNL FFPSMNDKKA LYLDVGQSLK IGAFSIDEGQ IFKERFYRND ELGGEAITLK
     MMEYCDDLFK RESKYSIQEN PLSMIKLRRA CEEVKAKLSD HDSWHLHIPK FYNNIDLNIP
     EFSKSLFEEL TLDVINRLIV EILEFMNKET FEYIIVCGKS TRIPKLKEMI RKLISTEQPE
     AEICDWIECP IELGGCIESY ISNDPNILMN DNTCCNYGIS NENGEMIVIV PRTSVPYSKT
     QTISIPLTGN EKFISIDIYE GNRKFVKDCE KIGTLRLDIP DNYQDAHFEV ELIFELFFSL
     NLNMTVSARS PTYGTEDSFI PSRPVPLKPE EIEELLLQMA SDTIPIMGTN SIGPTIDDLD
//