ID A0A1Y2D5E0_9FUNG Unreviewed; 579 AA.
AC A0A1Y2D5E0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DnaJ-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LY90DRAFT_669970 {ECO:0000313|EMBL:ORY54518.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY54518.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY54518.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY54518.1,
RC ECO:0000313|Proteomes:UP000193920};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY54518.1}.
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DR EMBL; MCOG01000084; ORY54518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2D5E0; -.
DR STRING; 1754190.A0A1Y2D5E0; -.
DR OrthoDB; 276132at2759; -.
DR Proteomes; UP000193920; Unassembled WGS sequence.
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; 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; 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; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43096:SF52; 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:UP000193920};
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 38..102
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 187..267
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 187..267
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 403..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 64219 MW; F19A54838454ADB1 CRC64;
MIYLNKIALL NNNNNNKIIQ NQKREFHATV PSRDSKRDLY EVLGIKKGAS PKEIKAAYYK
LAKLYHPDTN KSKEASEKFI EIQNAYEILS DDNKRAQYDQ YGHAAFDPNG AAGAGGFQGH
GGFGGFNGFD IFEQMFRGFG RAGGMGGFGN MGNMGGHYNS YSSHSYGMVG RDIKTTLTID
FMDVVKGTTK QLKYYHMVFC SDCDGMGTNN KSTPGKCPKC NGTGQEFIQH GGFGMARPCS
QCHGEGFFIP GDKRCKKCQG RRLIRKLDTV DVPIPKGVDS MVQLRLAGKG DAPVMGKGPF
GDLYIAVNIL PHPVFKREKN DVHVHVTLPL TKAILGGKVT IPTVDGDFEM DLHAGIQPEE
KKILRARGLY IMDTNVRGDE WIHFKVEIPK HLTKKQKEIL KSFQEEEEKK KGTKKNPSST
KKDQHHQENQ ANQTNQQTSQ KTKDQKKDEK SGTSTETHKG PKSEDTTNTT NATTNNNNNN
KTNTTKNSSS SSSHPNQGKK NDSSKRSYST TTSPISSNEE EGSSSSSAST SKVASEQKIE
KKEEEEAEDT AANKTTSKEP KEKEEDLSLF QKIKKIFIH
//
