ID A0A1U8ABR2_NELNU Unreviewed; 477 AA.
AC A0A1U8ABR2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Chaperone protein dnaJ 1, mitochondrial isoform X1 {ECO:0000313|RefSeq:XP_010259143.1};
GN Name=LOC104598665 {ECO:0000313|RefSeq:XP_010259143.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010259143.1};
RN [1] {ECO:0000313|RefSeq:XP_010259143.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_010259143.1; XM_010260841.2.
DR AlphaFoldDB; A0A1U8ABR2; -.
DR STRING; 4432.A0A1U8ABR2; -.
DR GeneID; 104598665; -.
DR KEGG; nnu:104598665; -.
DR eggNOG; KOG0715; Eukaryota.
DR InParanoid; A0A1U8ABR2; -.
DR OrthoDB; 276132at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
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; cd10747; DnaJ_C; 1.
DR Gene3D; 6.20.20.10; -; 2.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
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; 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; PTHR43096:SF36; CHAPERONE PROTEIN DNAJ 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 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; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00546}.
FT DOMAIN 91..156
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 218..292
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 218..292
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
SQ SEQUENCE 477 AA; 53263 MW; EBEA4AAC7C7EC608 CRC64;
MGRFNRLGFG QKSLFRARRH LLSSASNASP AYHGVRFGGA SVFQQVLFFA RNIYSCSLEV
SRRPDRFSTV EIRLMNRNFH ATGLCYSIER DFYEILGVPK DASQDEIKKA FHVLAKKYHP
DANKNNPSAK RKFQEIRDAY ETLRDSERRA QYDRVRTRGS GEGEYAAADA EDMNYSYQGH
FSDSFHKIFS EFFKDEAENF ATDIQVDLHL SFSEAAKGCI KDLSFNARVP CDSCNGHGYP
IGAKLRVCPT CKGIGRVTLP PFTSTCNSCK GSGQIIKEYC TTCRGSGVVE GVKEVKVTIP
AGVDYGDTIH VPKAGNSGGR GVQPGSLYIR LKVKKDPVFE RDGADIYVDS HISFTQAILG
GKVDVPTLSG KMQVEIPKGV QPGQLLVLRG RGLPKQGGFI NQGDQYVRFR INFPTSLNER
QRELIEEYAR DECNSGNNTS AEGNWWQQIV DQLAGSRFMV QVTLILLIFL FLNKTTS
//
