DNJH2_ALLPO
ID DNJH2_ALLPO Reviewed; 418 AA.
AC P42824;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DnaJ protein homolog 2;
DE Flags: Precursor;
GN Name=LDJ2;
OS Allium porrum (Leek) (Allium ampeloprasum var. porrum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Allioideae; Allieae; Allium.
OX NCBI_TaxID=4681;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bessoule J.J., Testet E., Cassagne C.;
RT "Cloning of a new isoform of a DnaJ protein from Allium porrum epidermal
RT cells.";
RL Plant Physiol. Biochem. 32:723-727(1994).
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}.
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DR EMBL; X77632; CAA54720.1; -; mRNA.
DR PIR; S42031; S42031.
DR AlphaFoldDB; P42824; -.
DR SMR; P42824; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
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; Zinc; Zinc-finger.
FT CHAIN 1..415
FT /note="DnaJ protein homolog 2"
FT /id="PRO_0000071077"
FT PROPEP 416..418
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396763"
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"
FT ZN_FING 135..219
FT /note="CR-type"
FT REGION 382..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 415
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 415
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 418 AA; 46584 MW; DCE2A4DF192329E6 CRC64;
MFGRAPKKSD NTKYYEVLGV SKNATPEDLK KAYRKAAIKN HPDKGGDPEK FKEIGQAYEV
LNDPEKREIY DQYGEEGLKE GMGGGGGVHD PFDIFQSFFG GGGFGGGGSS RGRRQRRGED
VVHPLKVSLE DLYNGTSKKL SLSRNVLCTK CKGKGSKSGA SMNCASCQGS GMKVSIRQLG
PGMIQQMQHP CNECKGTGEM ISDKDRCPQC KGEKVVQQKK VLEVHVEKGM QNGQKITFPG
EADEAPDTVT GDIVFVLQQK EHPKFKRKGD DLFYEHSLSL TEALCGFQFV LTHLDNRQLL
IKSNPGEVIK PDQFKGINDE GMPMYQRPFM RGKLYIHFSV DFPDSLTPDQ CKALESVLPS
RNASRLTDME IDECEETTMH DVNIEEEMRR KQHQQAQEAY DEDDEGHGGA QRVQCAQQ
