ID H0AAY9_HALSG Unreviewed; 507 AA.
AC H0AAY9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Chaperone protein DnaJ {ECO:0000313|EMBL:EHK02057.1};
DE Flags: Fragment;
GN ORFNames=HRED_05978 {ECO:0000313|EMBL:EHK02057.1};
OS Haloredivivus sp. (strain G17).
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC Candidatus Haloredivivus.
OX NCBI_TaxID=1072681 {ECO:0000313|EMBL:EHK02057.1, ECO:0000313|Proteomes:UP000003484};
RN [1] {ECO:0000313|EMBL:EHK02057.1, ECO:0000313|Proteomes:UP000003484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G17 {ECO:0000313|EMBL:EHK02057.1,
RC ECO:0000313|Proteomes:UP000003484};
RA Ghai R., Pasic L., Fernandez A.B., Martin-Cuadrado A.-B., Mizuno C.M.,
RA McMahon K.D., Papke R.T., Stepanauskas R., Rodriguez-Brito B., Rohwer F.,
RA Sanchez-Porro C., Ventosa A., Rodriguez-Valera F.;
RT "New Dominant Microbial Groups Along A Salinity Gradient.";
RL Sci. Rep. 0:0-0(2011).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK02057.1}.
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DR EMBL; AGNT01000099; EHK02057.1; -; Genomic_DNA.
DR AlphaFoldDB; H0AAY9; -.
DR PATRIC; fig|1072681.7.peg.574; -.
DR Proteomes; UP000003484; Unassembled WGS sequence.
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; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 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; 1.
DR InterPro; IPR002939; DnaJ_C.
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 PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43096:SF52; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00546};
KW Reference proteome {ECO:0000313|Proteomes:UP000003484};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00546}.
FT DOMAIN 58..139
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 58..139
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHK02057.1"
SQ SEQUENCE 507 AA; 56272 MW; 266122E208CFB2FE CRC64;
ETPKPRKRRL QTGRGQRQAA SNFQDLFEEI FGGGSRRQSR GQDMKINTTI SLGEAYNGVE
KTVKVSRNSQ CEACNGSGAE GGNTETCPEC NGEGRVREVE RSIFGRRQVV KECSRCSGRG
EIPEKDCSDC GGEGVREVEE TITFDIPAGV QDGQRLRLEG KGHENREGRS GDLYVFITVE
AHESLERRGS DLYTVKKIGV GDAALGWKFK EWNGLDKETD EVTLTMNEDK SIEALFEEDV
DVSIEDVSVP QTVDGDIDFN YQIANQQEEI TDNFTVRLNG REVSRTEKTV SKGETINEDG
PTVTPLAGDG SESAKLEIEY AGVKDSRSFR IASVQKEFVE GWNYFSLPIA TSQTMNIEEI
FDQDEINTIW TYENSWKNYY PGAPDNQFDT IRGGQGYIVE AEEDFSITPI VETNLSAVES
DDPVKPAQNN LDAGWNLIGS YWTTGIEASD TGAYSSLPED HITSTLYTDN DGSLSLQELG
NKDMEPSEAY WISSKEEAAY TKSQEAE
//
