ID C5LZA8_PERM5 Unreviewed; 420 AA.
AC C5LZA8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=DNAJ domain protein, putative {ECO:0000313|EMBL:EEQ97902.1};
GN ORFNames=Pmar_PMAR025526 {ECO:0000313|EMBL:EEQ97902.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EEQ97902.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG686856; EEQ97902.1; -; Genomic_DNA.
DR RefSeq; XP_002765185.1; XM_002765139.1.
DR AlphaFoldDB; C5LZA8; -.
DR EnsemblProtists; EEQ97902; EEQ97902; Pmar_PMAR025526.
DR GeneID; 9037716; -.
DR InParanoid; C5LZA8; -.
DR OMA; QHYNGEA; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
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; cd10747; DnaJ_C; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
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:SF10; DNAJ-LIKE-2, ISOFORM A; 1.
DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-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.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 27..88
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 378..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 46741 MW; 7182E26E9DF32550 CRC64;
MFFGGDPFED FAGMGSRRGG ADVDTQKYYD VLGVSKDATT AEIKKAFRKL AIKHHPDKGG
DADAFKEMTR AYEVLSDEEK RQRYDRFGED GVDQEGPSGG GMDMFDMMFG GGGNRSRRGK
RKGEDISHVL EVSLSQFYNG ATRKLAINRV VIDRSVPVKT CNACDGEGVV IKVVRMGPMI
QRVRQACPQC NGQGQSFKTK KSKEIIEVHI QKGMKDGQQI PFRGMADESD PSEEPGDFIV
VLKQKASQND ASAHGFTRKG NDLYLRKSIT LLEALTGYTT VIEHMDGRKL IVKSKKGEVI
KPVDMTAERH LLKCVKGEGM PSLQNQFVCG NLFIILDIVF PNEMKEKACK ELAKILPHPK
DAPKITSKMD KEYEHHQLVD MDPAESLRAQ QFGGSREAYD EDDDDNEGFP GAQRVQCAQQ
//