ID A0A0A1UBC1_ENTIV Unreviewed; 589 AA.
AC A0A0A1UBC1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Chaperone protein DNAK, putative {ECO:0000313|EMBL:ELP90911.1};
GN ORFNames=EIN_360740 {ECO:0000313|EMBL:ELP90911.1};
OS Entamoeba invadens IP1.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP90911.1, ECO:0000313|Proteomes:UP000014680};
RN [1] {ECO:0000313|EMBL:ELP90911.1, ECO:0000313|Proteomes:UP000014680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP1 {ECO:0000313|EMBL:ELP90911.1,
RC ECO:0000313|Proteomes:UP000014680};
RA Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB206483; ELP90911.1; -; Genomic_DNA.
DR RefSeq; XP_004257682.1; XM_004257634.1.
DR AlphaFoldDB; A0A0A1UBC1; -.
DR EnsemblProtists; ELP90911; ELP90911; EIN_360740.
DR GeneID; 14889847; -.
DR KEGG; eiv:EIN_360740; -.
DR VEuPathDB; AmoebaDB:EIN_360740; -.
DR OrthoDB; 1377056at2759; -.
DR Proteomes; UP000014680; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10170; HSP70_NBD; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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.
DR PROSITE; PS00329; HSP70_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 561..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 589 AA; 66150 MW; A4DE5E50AB251F3D CRC64;
MSDSMDNYIQ VGIDIGTTKC CICVVGQDGI PTVLEVDMTK LDHKELLPSY VSFIPNQVIV
GEAVKKMTQT SNVLYDPKRL LGLSLEEIPE DEKKSFTFDI DEINNRIVYM VENGNKNNEP
EPFRPEEVTA FLVQTLFAKL EEIPEYRNKK KKYVVTHPVS FNENQINYAE MVMHLVGITT
FKFLPEPIAA LLSMKTMMSE IKVNEKVLVL DVGGGTLDVT ICSLKKSGYF ECEACNGDFN
VGGNAVDRAV SELIIAKTAN IEDYSTYFSE PKRALITEKI AYQKKKARLR VESERVKILL
SSNEVVEVNL SFLFDSTVGY VMEISRAEMN EKCSDLFAKY VRCIKQTLIE NNVNSRGIKK
VIMTGGASEM IALQDQAKLI FKEAAVFVVD TPELAVVKGA SMYHKGDIQN VINHSDEDIR
VEIGSKCEVI VSKTDLLPAE GTKRVATVVD GQKKAVFKIY KGDNSQADFN TFVGEFVFDN
IPIQKAGDVV FVLKIGVDTV GNIEAEAHMI NGRTERIKAT VSFEKNKEDF IFTKRHFDYK
AYNWISAHPE EKRPSSVSSR FCWILIFVLL NSLLVMYLIG VGQNRVFAS
//
