ID A0A1Y2F644_9FUNG Unreviewed; 532 AA.
AC A0A1Y2F644;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=DnaJ-domain-containing protein {ECO:0000313|EMBL:ORY79137.1};
GN ORFNames=LY90DRAFT_664765 {ECO:0000313|EMBL:ORY79137.1};
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:ORY79137.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY79137.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY79137.1,
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:ORY79137.1}.
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DR EMBL; MCOG01000015; ORY79137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2F644; -.
DR STRING; 1754190.A0A1Y2F644; -.
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; 1.
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; 1.
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 86..150
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 235..315
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 235..315
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 425..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 59269 MW; 0C4B162CFEE713E5 CRC64;
MSSQITSSIP KVQTIVNSTI INQSAHAISS VTNSLNCPQS IKLNGKRNFS LDTSSYALLN
NKNKKIIQSQ KREFHATVPS RESKKDLYEV LGVKKGASAK EIKSAYYKLA KTYHPDTNKS
KEANEKFIEI QNAYEILSDD KKRAQYDQFG HAAFDPNGAA GAGGFQGRGG FGGFSGFDIF
EQMFRGFGRA GGMGGFGNMG NMGGHYDPYS NRTYGMLGRD IKTTLTIDFM DVVKGTTKQL
NYHHMVFCSD CDGMGTNNKS TPGKCPKCNG SGQEFIQHGG FGMARPCSQC HGEGFFIPHD
KRCKKCEGKR LIRKLDTVDV PIPKGVDSMV QLRLAVFKRE KNDVHVNVTL PLTKAILGGK
VTIPTVDGDF EMDLPAGIQP EEKKILRARG LYVMDTNVRG DEWIHFKVEI PKHLTKKQKE
LLKSFQEEEE KKHPFKKAKQ AYQQAKAQKK NSKTTSTTNS SSSTTESKKE SNNTSTNTNT
TNTNTTTSNN NNTKNNTTFN SVNPKNDKKN DSPKQSRDKE KKYMYLYISY NN
//
