ID   A0A1I8FZ24_9PLAT        Unreviewed;       827 AA.
AC   A0A1I8FZ24;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Heat shock protein {ECO:0000313|WBParaSite:maker-uti_cns_0000343-snap-gene-1.11-mRNA-1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0000343-snap-gene-1.11-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0000343-snap-gene-1.11-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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DR   AlphaFoldDB; A0A1I8FZ24; -.
DR   WBParaSite; maker-uti_cns_0000343-snap-gene-1.11-mRNA-1; maker-uti_cns_0000343-snap-gene-1.11-mRNA-1; maker-uti_cns_0000343-snap-gene-1.11.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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; 1.
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          506..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          755..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..778
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   827 AA;  90455 MW;  0E799316E8C7D622 CRC64;
     MAIAVVGFDM GYLNSFVAVA RAGGIETVAN EYSDRCTASC VSFSDSIRFI GNSAKQRVLT
     NPRDTIHGFT RFLGKNFDDP SVQAELPFTP YNLVKLENGS VGFKVNYLNE EATFSAEQVA
     AMLLTKLKTV AQSNLGTPVV DCVLNVPTYW TDRERRALLD ATHIAGLNCL KLINDLTAIG
     LNYGIYKKDL PAVDKPSKNV AFVDMGHNHL QVAVIAFNEG QMRVLATASD PSLGGRDFDR
     AIFSHFADDI KQRFKLDVRS NAKATMRLLE ECSKVKKLMS ANSTDIPLNI ECLMQDRDVN
     GRINRETFNG LLDSAGLLVR VEQCLSRCLT LAKLQPKDIA SVELVGGSTR VPAVKDLVTK
     VFGQSPMTTL NADEAVARGC ALMCAILSPA FKVREFSISD WQPYSISLSY RDADGKDDSV
     EVFPEGYQFP MSRTLTFYRK AAFELAAHYT NPQAVPTPLI GKFSVGNVQP SPSGEAARIK
     VKVRLNSHGI FTVSQAKLAE TVEKVVDEPE EKMETDAPAE SAEVVAEAEA APGGTAADSA
     GSPMEVGADQ AERQQQQAAA PADPKKSAEK KTKKVTRYTD LPIDADCVKQ LSKKLLTDFQ
     EREANMVLQE TREHERCLAR NTVEEYVYEM RDKLSSVLEQ FVSEAERESY SQLLTATEDW
     IYGDGENLAK QAYVDKLAEL RGPGERFLRR AKEFEERPRA ADALGHALQH ARKAKQQWLI
     TQQNEQNRLA ANQDPSLTSA DIRSQHSALE SAVNPILNKP KPQPPKVEEP PPQQQQPQAS
     TQPPADGAAG PDATAQDGDQ NAAPGSAKKS TSGGAKVNGK EADMDLD
//