ID   A0A0R3RFJ2_9BILA        Unreviewed;       855 AA.
AC   A0A0R3RFJ2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Heat shock 70 kDa protein 4L {ECO:0000313|WBParaSite:EEL_0000013201-mRNA-1};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000013201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000013201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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DR   AlphaFoldDB; A0A0R3RFJ2; -.
DR   STRING; 1147741.A0A0R3RFJ2; -.
DR   WBParaSite; EEL_0000013201-mRNA-1; EEL_0000013201-mRNA-1; EEL_0000013201.
DR   Proteomes; UP000050640; Unplaced.
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:0006950; P:response to stress; IEA:UniProt.
DR   CDD; cd10228; HSPA4_like_NDB; 1.
DR   Gene3D; 1.20.1270.10; -; 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; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR45639:SF4; HSC70CB, ISOFORM G; 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; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   REGION          520..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          804..855
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..837
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   855 AA;  96547 MW;  05DDAB35B92E02D5 CRC64;
     MSVVGFDFGN INSFIAVARQ GGIETITNDY SLRATPSCVA FTTRGRSMGV AARQQLNTNI
     KNTIINFKHL LGRKFSDQVT QKYRKFVPCE MVQLPNDEIG LKVQYFNEER VFTPEQVVAT
     FLVKLKDITE NSSQGMRNVT DCVVSVPFYF ADTQRRALLT AVRIAGLNCL QILNETTAVA
     LAYGIYKQDL PAENEPPRIV AFVDIGHSAA QAVLVAYNKG KLTVLGATFD LEVGGLAFDD
     VIRDHFSKLF YDTYKIDVSS NKRAWFRLLD ECEKIKKQMS TNSTAIPLNI ECFMNDMDVT
     GKMQRSQFEE LAQPLLDRVR LLLTNLLKEC GKKAEEVESV ELVGGTSRIP VIKKITAEVF
     GKEPKTTMNQ DEAVARGAAM KCAILSPAFK VRDFSVKDSQ PYRIKLSWAA VGQSEGGEND
     VFIEHDEFPY SKMLTLYRQE PFQVDASYSY PNQIPHPIRH IGMCQALRTL PTGSWVVKNI
     TPGPNNEPRK VKVKVRINPN GIFSVCSANT FETIEAGPLD TQAQKASEAM ETDDSKGNQD
     KEENADATTN NVVPPVEEDQ KLLNNSGPKT KTITVDLPVE EHVPCIIANE PQLIQFEASF
     FFIRSKILEI SIGKPACEYL LIFKKEMQGK DRVEKEKADA KNAVEEYVYY IRDKLSDVFA
     EFISNDDADK LRDLLTKTED WLYDEGEDVE RKVYDAKMSE LKKLGDPVQE RHREYENRKN
     AFDEFDRTIM RARKAYDEYT KGSEKYAHLG SSDMEKVISA VEEKKKWVDD QRSRQEIRKK
     TEPPIVFVHQ IQDEQQKFEN IILPILNKPK PAPAKTEPAK EPEKGSEGQK GENPASDRAP
     KADANNVNEL GMEVD
//