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Database: UniProt
Entry: A0A0N4Z1P7_PARTI
LinkDB: A0A0N4Z1P7_PARTI
Original site: A0A0N4Z1P7_PARTI 
ID   A0A0N4Z1P7_PARTI        Unreviewed;       776 AA.
AC   A0A0N4Z1P7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:PTRK_0000079300.1};
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_0000079300.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000079300.1}
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; A0A0N4Z1P7; -.
DR   STRING; 131310.A0A0N4Z1P7; -.
DR   WBParaSite; PTRK_0000079300.1; PTRK_0000079300.1; PTRK_0000079300.
DR   Proteomes; UP000038045; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   REGION          516..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   776 AA;  87618 MW;  C59A56B0A14B2D02 CRC64;
     MAVVGFDFGN LNCYIAVARQ GGIDVITNDY SLHATPACVA FGNKDRVSGV GARQKVNTNF
     KSTVLNFKQL LGLKFSDPRA QKMKRFIPCE MVQLEDDNIG LKVNYLGEWQ ILTPEQIAAA
     LFVKLKSITE QACSEIKCVS DLVVSIPPYF TDIQRRALKV AVDLTGMNCL KLVNENSAAA
     SAYGIYKSDL PVEGNPPRIV AIIDGGHTSV QATLCSFNKG KCEIIGYTYD TDVGGLYFDD
     CIREHFRKMF IEKYKIDAET NPRSWLRLLD ECEKIKKQMS TNSIAMPLNI ECFMNDIDVS
     GKMSRDEFEH VAGPLFEKIK NILHKLFEET GYTPDKVNEV EIIGGSSRVP LFRKIVKDVF
     GKEPKTTMNQ DDSISRGAAL QCAILSPAVR VRDFSLYERL GNQVVIKYGD SNDLKSLWKG
     NAEIGSSKLI TTFRKEDFII DGLYNAPYEV QPQNFIGRWI IKGVTPNSDG GEKKIKVKAG
     VDYSGIFNVF GATAYEIVPL SKEELEAEAA AKAAEAAKAA ATSNEEKKEG DETKKEADNK
     KKENEEEKVK EEPAIKTKTI TTELIIEAQI PYQFNVLKAR EFEFKMQQTD LLEKQKADAK
     NAVEEYVYNM RDKLCETLSE FIQENDAEEF KSLLQKTEDW LYEDGEDAET KVYEEKLSFL
     KKYGDPVVER YQEFESRAIS FEAIEHKIMQ VDKFIDQYSA GVEAYSHIDE TDVKKVQDAV
     EEKRRWVWDN KDKQAKKAKY DAPHVWSHEI NSAKASLDSI VNPIMNKPKP KQEASS
//
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