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Database: UniProt
Entry: A0A183K209_9TREM
LinkDB: A0A183K209_9TREM
Original site: A0A183K209_9TREM 
ID   A0A183K209_9TREM        Unreviewed;       401 AA.
AC   A0A183K209;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=DnaJ subfamily A member 1 {ECO:0000313|WBParaSite:SCUD_0000902201-mRNA-1};
GN   ORFNames=SCUD_LOCUS9022 {ECO:0000313|EMBL:VDP33705.1};
OS   Schistosoma curassoni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0000902201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SCUD_0000902201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP33705.1, ECO:0000313|Proteomes:UP000279833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dakar {ECO:0000313|EMBL:VDP33705.1}, and Dakar, Senegal
RC   {ECO:0000313|Proteomes:UP000279833};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC       anchor {ECO:0000256|ARBA:ARBA00004635}.
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DR   EMBL; UZAK01033023; VDP33705.1; -; Genomic_DNA.
DR   STRING; 6186.A0A183K209; -.
DR   WBParaSite; SCUD_0000902201-mRNA-1; SCUD_0000902201-mRNA-1; SCUD_0000902201.
DR   Proteomes; UP000050789; Unplaced.
DR   Proteomes; UP000279833; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   CDD; cd10719; DnaJ_zf; 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   HAMAP; MF_01152; DnaJ; 1.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
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; 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:UP000279833};
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          6..68
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          121..205
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         121..205
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          362..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  45117 MW;  C1E5A9FB357E73F6 CRC64;
     MVKERKYYDL LGVPVTATEA EIKKAYRQKA LKYHPDKNPD SADKFKEISQ AFMVLSDPEK
     RELYDARGEQ GIKEGGVDSG GMADPMDIFQ MFFGGGRSRG PRRGKDCVHQ LSVTLEELYN
     GSVRKLGVTR KVICDQCQGR GGKAGAVVTC RTCRGTGIQT HVRQLNVGFV QQIQTTCSAC
     KGEKEIIDPK DCCKKCEGRK VVRETKVIEV PIDKGMTDGQ TIKFHDEGDR EPGLEPGDLI
     ITLDEQPHSR FIRRRNDLIH TIELSLSEAL CGFQRTIRSL DDRTLVITSR PGEVYTNKDF
     RAIEGEGMPR YKNPFDKGRL IIKFDISFPK NGFLSKTQLD SLRKLLPPPT CIEDIPEDAE
     SVELHPFDPE FDHQQQERRG EVYEDVDGSE SSNPRVQCAS A
//
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