DNJH1_ALLPO
ID DNJH1_ALLPO Reviewed; 397 AA.
AC Q03363;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=DnaJ protein homolog 1;
DE Short=DNAJ-1;
DE Flags: Precursor; Fragment;
GN Name=DNAJ1;
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].
RX PubMed=8495747; DOI=10.1016/0014-5793(93)81446-7;
RA Bessoule J.J.;
RT "Occurrence and sequence of a DnaJ protein in plant (Allium porrum)
RT epidermal cells.";
RL FEBS Lett. 323:51-54(1993).
CC -!- FUNCTION: Plays a continuous role in plant development probably in the
CC structural organization of compartments.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
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DR EMBL; X69436; CAA49211.1; -; mRNA.
DR PIR; S33312; S33312.
DR AlphaFoldDB; Q03363; -.
DR SMR; Q03363; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
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..394
FT /note="DnaJ protein homolog 1"
FT /id="PRO_0000071076"
FT PROPEP 395..397
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396762"
FT DOMAIN <1..52
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REPEAT 127..134
FT /note="CXXCXGXG motif"
FT REPEAT 143..150
FT /note="CXXCXGXG motif"
FT REPEAT 170..177
FT /note="CXXCXGXG motif"
FT REPEAT 186..193
FT /note="CXXCXGXG motif"
FT ZN_FING 114..198
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT REGION 367..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 394
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 394
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 397 AA; 44169 MW; 33BA6B981586EFAB CRC64;
KNASPDDLKK AYRKAAIKNH PDKGGDPEKF KELAQAYDVL SDPEKREIYD QYGEDALKEG
MGGGGGDHDP FDIFQSFFGG GGFGGGGSSR GRRQRRGEDV VHPLKVSLEE LYNGTSKKLS
LSRNVICSKC NGKGSKSGAS MRCASCQGSG MKVSIRQLGP GMIQQMQHPC NDCKGTGEMI
NDKDRCPLCK GEKVVQEKKV LEVHVEKGMQ NGQRITFPGE ADEAPDTVTG DIVFVLQQKE
HPKFQRKGDD LFYKHTLSLT EALCGFQFVL THLDGRQLLI KSNPGEVVKP DQFKAINDEG
MPMYQRPFMR GKLYIQFLVD FPDSLTPDQC KVIESVLPRS ASSQLTDMEI DECEETTMHD
VNIEEEMRRK QHQHAQEAYD EDDEGHGGGQ RVQCAQQ
