DNJH_ATRNU
ID DNJH_ATRNU Reviewed; 417 AA.
AC P43644;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=DnaJ protein homolog ANJ1;
DE Flags: Precursor;
OS Atriplex nummularia (Old man saltbush) (Atriplex johnstonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Atripliceae; Atriplex.
OX NCBI_TaxID=3553;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8467224; DOI=10.2307/3869601;
RA Zhu J.K., Shi J., Bressan R.A., Hasegawa P.M.;
RT "Expression of an Atriplex nummularia gene encoding a protein homologous to
RT the bacterial molecular chaperone DnaJ.";
RL Plant Cell 5:341-349(1993).
CC -!- FUNCTION: Plays a continuous role in plant development probably in the
CC structural organization of compartments. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: By heat shock, and in response to NaCl stress.
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DR EMBL; L09124; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; JQ2142; JQ2142.
DR AlphaFoldDB; P43644; -.
DR SMR; P43644; -.
DR GO; GO:0016020; C: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 Chaperone; Lipoprotein; Membrane; Metal-binding; Methylation; Prenylation;
KW Repeat; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..414
FT /note="DnaJ protein homolog ANJ1"
FT /id="PRO_0000071088"
FT PROPEP 415..417
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396766"
FT DOMAIN 11..76
FT /note="J"
FT REPEAT 148..155
FT /note="CXXCXGXG motif"
FT REPEAT 164..171
FT /note="CXXCXGXG motif"
FT REPEAT 191..198
FT /note="CXXCXGXG motif"
FT REPEAT 207..214
FT /note="CXXCXGXG motif; approximate"
FT ZN_FING 135..219
FT /note="CR-type"
FT REGION 384..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 414
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 414
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 46566 MW; BA597AEEA3A22667 CRC64;
MFGRAPKKSD STRYYEILGV PKDASPEDLK KAYKKAAIKN HPDKGGDPEK FKELAHAYEV
LSDPEKREIY DQYGEDALKE GMGGGGGMHD PFDIFQSFFG GSPFGGVGSS RGRRQRRGED
VVHPLKVSLE DLFTGTTKKL SLSRNVICSK CTGKGSKSGA SMKCSGCQGT GMKVSIRHLG
PSMIQQMQHP CNECKGTGET INDKDRCPQC KGEKVVQEKK VLEVVVEKGM QHGQKITFPG
EADEAPDTVT GDIVFVLQQK EHPKFKRKGE DLFYEHTLSL TEALCGFRFV LTHLDGRQLL
IKSNLGEVVK PDQFKAIEDE GMPIYQRPFM KGKMYIHFTV EFPDSLNPDQ VKSLEAILPP
KPSMSLTYME LDECEETTLH NVNIEEEMKR KQTQAQQEAY DEDDEPAGGQ RVQCAQQ