DNJA1_DICDI
ID DNJA1_DICDI Reviewed; 459 AA.
AC Q54ED3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=DnaJ homolog subfamily A member 1 homolog;
DE Flags: Precursor;
GN Name=dnaja1; ORFNames=DDB_G0291568;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Co-chaperone for Hsp70 family members. Plays a role in
CC protein transport into mitochondria and in the regulation of apoptosis
CC via its role as co-chaperone (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Cytoplasm {ECO:0000250}. Microsome {ECO:0000250}.
CC Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and
CC associated with microsomes. A minor proportion is associated with
CC nuclei and mitochondria (By similarity). {ECO:0000250}.
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DR EMBL; AAFI02000177; EAL61768.1; -; Genomic_DNA.
DR RefSeq; XP_635307.1; XM_630215.1.
DR AlphaFoldDB; Q54ED3; -.
DR SMR; Q54ED3; -.
DR STRING; 44689.DDB0233607; -.
DR PaxDb; Q54ED3; -.
DR EnsemblProtists; EAL61768; EAL61768; DDB_G0291568.
DR GeneID; 8628251; -.
DR KEGG; ddi:DDB_G0291568; -.
DR dictyBase; DDB_G0291568; dnaja1.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; Q54ED3; -.
DR OMA; GMSAFNG; -.
DR PhylomeDB; Q54ED3; -.
DR Reactome; R-DDI-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR PRO; PR:Q54ED3; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
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:0042026; P:protein refolding; IBA:GO_Central.
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 3: Inferred from homology;
KW Chaperone; Cytoplasm; Endoplasmic reticulum; Lipoprotein; Membrane;
KW Metal-binding; Methylation; Microsome; Mitochondrion; Nucleus; Prenylation;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..456
FT /note="DnaJ homolog subfamily A member 1 homolog"
FT /id="PRO_0000328579"
FT PROPEP 457..459
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396756"
FT DOMAIN 6..73
FT /note="J"
FT REPEAT 171..178
FT /note="CXXCXGXG motif"
FT REPEAT 188..195
FT /note="CXXCXGXG motif"
FT REPEAT 215..222
FT /note="CXXCXGXG motif"
FT REPEAT 231..238
FT /note="CXXCXGXG motif"
FT ZN_FING 158..243
FT /note="CR-type"
FT REGION 405..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 456
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 456
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 459 AA; 50096 MW; B98F7F0C24B71466 CRC64;
MVKEKEYYER LGVKPDCTED ELKKAYRKMA VKYHPDKNQG PGKDAAEAKF KDISEAYEVL
SDPEKRKMYD SYGSEGMKES GFHASSAEDL FSHFFGAGGG GGGFSFGGGG GDDFGGFSFG
NMGGMGGMGG MGGGHKKRRK GEDIEHEMNR SLEELYNGKL VKISISRDEV CKTCKGSGSN
KPGVTTTCPT CNGSRYVFQK KQVGPGMIQQ VQTACHTCHG TGEKIKEEDK CKECKGKRVI
QGKKIVQFQV EKGTRDGERI MLQGQGSEYP GVPPGDVIIT IREKPNVNFK RNGDNLIYTK
RLKLLDSIAG SQFIINTLDQ RKLWVNHEKG DIIKQGDMRY IENEGMPIKG TSRKGKLIIA
FDIEYPSNLT NDDIEKLSKI LPKAATPSVS KSDCKSVGLS KVNFNTNEQS SHGGAGGAYQ
QHGGAYGHQK QQQQGFNPAD FGAQFGGGGP QQAQQCQQQ
