ID   Q8MUA7_HETGL            Unreviewed;       659 AA.
AC   Q8MUA7;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   13-SEP-2023, entry version 88.
DE   SubName: Full=Heat shock protein 70-C {ECO:0000313|EMBL:AAM93256.1};
OS   Heterodera glycines (Soybean cyst nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC   Heterodera.
OX   NCBI_TaxID=51029 {ECO:0000313|EMBL:AAM93256.1};
RN   [1] {ECO:0000313|EMBL:AAM93256.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kovaleva E.S., Chitwood D.J.;
RT   "Plant parasitic nematode heat shock protein 70-C.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAQ89579.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kovaleva E.S.;
RT   "Heat shock protein 70 from plant-parasitic nematode.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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   EMBL; AF529194; AAM93256.1; -; mRNA.
DR   EMBL; AY380802; AAQ89579.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MUA7; -.
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   2: Evidence at transcript level;
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};
KW   Stress response {ECO:0000313|EMBL:AAM93256.1}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..659
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007714161"
FT   REGION          607..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          283..310
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        614..631
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   659 AA;  72827 MW;  534120494425E428 CRC64;
     MKKSFVSFLF FTALLVIVCS KEEEGGAKEK KYGTIIGIDL GTTYSCVGVY KNGRVEIIAN
     DQGNRITPSY VAFTPDSGER LIGDAAKNQL TLNPENTIFD AKRLIGREFT DKTVQDDMKL
     WPFKIYNKAN KPHVQVKVGN EDKQFAAEEV SAMVLTKMKE IAESYLGHEV KNAVVTVPAY
     FNDAQRQATK DAGTIAGLNV VRIINEPTAA AIAYGLDKKE GERNILVFDL GGGTFDVSLL
     TIDNGVFEVL ATNGDTHLGG EDFDPRTIEY FIKLIKKKTG KDLRKDNRAV QKLRREVEKA
     KRALSVQHQV KLEVESLIDG EDFSETLTRA KFEELNMDLF RGTLKPVQKV LEDADLKKED
     IHEVVLVGGS TRIPKVQQLL KEFFNGKEPS RGINPDEAVA YGAAVQAGVI SGEENSEIVL
     LDVNPLTMGI ETVGGVMTKL ITRNTVIPTK KSQIFSTAAD NQPTVTIQVF EGERPMTKDN
     HLLGKFDLTG IPPAPRGVPQ IEVTFEIDVN GILHVTAEDK GTGNKNKITI TNDHNRLSPE
     EIERMINDAE KFAEEDKKTK EVVEARNEFE SYAYSLKNQL GDSEKLGGKL SAEDKTTIEG
     AVDEAISWLD SNKDAPPEEL KERKKDLEAK VQPIISKLYA GQSPPPGSEP PPTEEKDEL
//