ID   DNJH_CUCSA              Reviewed;         413 AA.
AC   Q04960;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=DnaJ protein homolog;
DE   AltName: Full=DNAJ-1;
DE   Flags: Precursor;
GN   Name=DNAJ1;
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=8342953; DOI=10.1006/abbi.1993.1389;
RA   Preisig-Mueller R., Kindl H.;
RT   "Plant dnaj homologue: molecular cloning, bacterial expression, and
RT   expression analysis in tissues of cucumber seedlings.";
RL   Arch. Biochem. Biophys. 305:30-37(1993).
CC   -!- FUNCTION: Plays a continuous role in plant development probably in the
CC       structural organization of compartments.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings in all tissues, but
CC       exceedingly high levels in hypocotyledons and roots.
CC   -!- INDUCTION: By heat shock; weakly.
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DR   EMBL; X67695; CAA47925.1; -; mRNA.
DR   PIR; S35581; S35581.
DR   AlphaFoldDB; Q04960; -.
DR   SMR; Q04960; -.
DR   STRING; 3659.XP_004169945.1; -.
DR   PRIDE; Q04960; -.
DR   EnsemblPlants; KGN52169; KGN52169; Csa_5G613470.
DR   Gramene; KGN52169; KGN52169; Csa_5G613470.
DR   eggNOG; KOG0712; Eukaryota.
DR   OMA; GMSAFNG; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10719; DnaJ_zf; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   HAMAP; MF_01152; DnaJ; 1.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR044713; DNJA1/2-like.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR43888; PTHR43888; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 2.
DR   SUPFAM; SSF57938; SSF57938; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Chaperone; Lipoprotein; Membrane; Metal-binding;
KW   Methylation; Prenylation; Repeat; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..410
FT                   /note="DnaJ protein homolog"
FT                   /id="PRO_0000071089"
FT   PROPEP          411..413
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396767"
FT   DOMAIN          10..75
FT                   /note="J"
FT   REPEAT          146..153
FT                   /note="CXXCXGXG motif"
FT   REPEAT          162..169
FT                   /note="CXXCXGXG motif"
FT   REPEAT          189..196
FT                   /note="CXXCXGXG motif"
FT   REPEAT          205..212
FT                   /note="CXXCXGXG motif"
FT   ZN_FING         133..217
FT                   /note="CR-type"
FT   REGION          387..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..404
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         410
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           410
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  46064 MW;  BB4C0FE990561616 CRC64;
     MFGRPKKSDN TKYYEILGVS KNASQDDLKK AYRKAAIKNH PDKGGDPEKF KELAQAYEVL
     SDPEKREIYD QYGEDALKEG MGGGGGHDPF DIFQSFFGGS PFGGGGSSRG RRQRRGEDVI
     HPLKVSLEDL YNGTSKKLSL SRNVICSKCK GKGSKSGASM KCPGCQGSGM KVSIRHLGPS
     MIQQMQHPCN ECKGTGETIN DKDRCSQCKG EKVVQEKKVL EVIVEKGMQN AQKITFPGEA
     DEAPDTVTGD IVFVLQQKEH PKFKRKGDDL FVEHTLSLVE SLCGFQFILT HLDGRQLLIK
     SLPGEVVKPD QFKAINDEGM PMYQRPFMKG KLYIHFSVEF PDSLNPEQCK ALEGVLPPRT
     SVQLSDMELD ECEETTLHDV NIEEEMRRKQ AQEAYDEDED MHGGAQRVQC AQQ