ID A0A016VWJ2_9BILA Unreviewed; 667 AA.
AC A0A016VWJ2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chaperone protein DnaK {ECO:0008006|Google:ProtNLM};
GN Name=Acey_s0003.g1184 {ECO:0000313|EMBL:EYC31691.1};
GN Synonyms=Acey-hsp-6 {ECO:0000313|EMBL:EYC31691.1};
GN ORFNames=Y032_0003g1184 {ECO:0000313|EMBL:EYC31691.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC31691.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC31691.1}.
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DR EMBL; JARK01001339; EYC31691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016VWJ2; -.
DR STRING; 53326.A0A016VWJ2; -.
DR Proteomes; UP000024635; 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 GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR CDD; cd11733; HSPA9-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 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:UP000024635}.
FT REGION 644..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 72223 MW; AAF54999A9F71D1A CRC64;
MLIPAARTFF NASAACSRVI ARTSYLNGIS QRFKSDAIRG AVIGIDLGTT NSCVAVMEGK
QAKVIENAEG VRTTPSTVAF TKDGERLVGA PAKRQAVTNP QNTLYATKRL IGRRFDDAEV
QKDVKIVPFK IVKASNGDAW VEAQGKMYSP SQVGAFVLMK MKETAENYLG TTVHNAVVTV
PAYFNDSQRQ ATKDAGQIAG LNVLRVINEP TAAALAYGLE KTEDKIIAVY DLGGGTFDIS
VLEIQKGVFE VKSTNGDTFL GGEDFDHALV NHLVAEFKRE QGVDLTKDPM AMQRLREAAE
KAKCELSSTT QTDINLPYLT MDASGPKHMT MKLTRAKFEQ LVGDLIKRTV EPCRKAMHDA
EVKPSDISEV LLVGGMSRMP KVQQTVQEVF GKAPSKAVNP DEAVAMGAAI QGAVLAGDVT
DVLLLDVTPL SLGIETLGGV MTKLIARNTT IPTKKSQVFS TAADGQTQVQ IKVCQGEREM
ANDNKLLGQF SLVGIPPAPR GVPQIEVTFD IDANGIVNVS ARDRGTGKEQ QIVIQSSGGL
SKDQIENMIK EAERNAAEDA KKKEMVEVLN QAESIIHDTE SKMTEFADQL PKEESEALKK
KIEETKTILA NKDNEKPETI KEAVSSLQQQ SLKLFEAAYK KMAEKNAGGA SDAQEAKTAE
EPKKEQN
//