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Database: UniProt
Entry: W1QC87_OGAPD
LinkDB: W1QC87_OGAPD
Original site: W1QC87_OGAPD 
ID   W1QC87_OGAPD            Unreviewed;       476 AA.
AC   W1QC87;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p {ECO:0000313|EMBL:ESW98149.1};
GN   ORFNames=HPODL_03796 {ECO:0000313|EMBL:ESW98149.1};
OS   Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS   Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW98149.1, ECO:0000313|Proteomes:UP000008673};
RN   [1] {ECO:0000313|EMBL:ESW98149.1, ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RX   PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA   Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA   Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA   Skryabin K.G.;
RT   "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT   DL1.";
RL   BMC Genomics 14:837-837(2013).
RN   [2] {ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RA   Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA   Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT   "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL   Submitted (OCT-2013) 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:ESW98149.1}.
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DR   EMBL; AEOI02000008; ESW98149.1; -; Genomic_DNA.
DR   RefSeq; XP_013934032.1; XM_014078557.1.
DR   AlphaFoldDB; W1QC87; -.
DR   STRING; 871575.W1QC87; -.
DR   GeneID; 25773230; -.
DR   KEGG; opa:HPODL_03796; -.
DR   eggNOG; KOG0715; Eukaryota.
DR   HOGENOM; CLU_017633_0_3_1; -.
DR   OMA; CPECAGD; -.
DR   OrthoDB; 276132at2759; -.
DR   Proteomes; UP000008673; Chromosome V.
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:UP000008673};
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          51..115
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          196..277
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         196..277
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
SQ   SEQUENCE   476 AA;  51503 MW;  6CC388AE9CB69331 CRC64;
     MNSVLKVRLL PRRLIWNAQS RYVRHARPLI FHGIRSACRE FHSSRPTQLE DPYKTLGVSQ
     SASASDIKKA YYKLAKKYHP DVNKEEGAEK KFHQLQEAYD ILSDPQKKQQ YDQFGAAAFD
     PNAGSGAGGF GGAHGGNPFA GFQGGFQGGN PFEGFGFNFE DLFGGMGGGR QRGVQHFQGE
     DVEVLKTISF REAIFGTRTS IDYRAVCQCD ACSGSGLKRN RKKSTCRSCD GTGSQVYQLQ
     AGFQMASTCK ACGGSGVFIN PSDACSSCHG EGVVDQHRQT EVNLPKGIKD GSRIRVSGAG
     NAPHTTTSKG TVLSNGDLII RIKVAPDPEF VRDGVNVIYN CKIAMTTAAL GGTVEIPTLE
     GQKVKIKIPA GSEHGKVITI PERGVPYAGN RRGDLRVVLN VVPLKPQNAT QTALLEALAD
     AFGDNTANRM DPSWKPLESV DKESSAGANC EHPSNLRRIE SFLSNAFKKI LNKDDK
//
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