ID A0A0N4Z0J3_PARTI Unreviewed; 658 AA.
AC A0A0N4Z0J3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Heat shock protein 70 {ECO:0000313|WBParaSite:PTRK_0000022300.1};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000022300.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0000022300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR AlphaFoldDB; A0A0N4Z0J3; -.
DR STRING; 131310.A0A0N4Z0J3; -.
DR WBParaSite; PTRK_0000022300.1; PTRK_0000022300.1; PTRK_0000022300.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..658
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005890913"
FT REGION 636..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 281..308
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 658 AA; 72567 MW; 13C41A06F4315FBB CRC64;
MKLTYLFGFI TLLAIGQVYS DEENSKENKY GTIIGIDLGT TYSCVGVYKN GRVEIIANDQ
GNRITPSYVA FTPDSGERLI GDAAKNQLTS NPENTIFDAK RLVGREFSDK SVQADMKLWP
FTVIDKNNKP HVQVNVGTEK KTFTAEEVSA MVLTKMKEIA ETYLGKEVKN AVITVPAYFN
DAQRQATKDA GTIAGLNVVR VINEPTAAAI AYGLDKKEGE KNILVFDLGG GTFDVSLLTI
DNGVFEVLAT NGDTHLGGED FDQRVMEYFI KLYKKKTGKD IRKDNRAVQK LRREVEKAKR
ALSVQHQVKV EVESLFEGED FSETLSRSKF EELNMDLFRA TMKPVQKVLE DADLKKTDVH
EIVLVGGSTR IPKVQQLIKE FFNGKEPSRG INPDEAVAYG AAVQGGVISG EDSTSGIVLL
DVNPLTLGIE TVGGVMTKLI PRNTVIPTKK SQVFSTAADN QPTVTIQVFE GERPMTKDNH
QLGKFDLTGI PPAPRGVPQI EVTFEIDVNG ILHVTAEDKG TGSKNKITIT NDQNRLSPED
IERMINDAEK FADEDKKLKE VVESRNELEG YAYNLKNQIG DTEKLGGKLS DEEKVTIETA
VDQAINWLES NKDATAEELQ QQKKDLEGTV QPIISKLYQG ADGGTPPTDE ENADKDEL
//
