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Database: UniProt
Entry: S9PWK7_SCHOY
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Original site: S9PWK7_SCHOY 
ID   S9PWK7_SCHOY            Unreviewed;       516 AA.
AC   S9PWK7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=DNAJ domain-containing protein Mdj1 {ECO:0000313|EMBL:EPX71863.1};
GN   ORFNames=SOCG_03799 {ECO:0000313|EMBL:EPX71863.1};
OS   Schizosaccharomyces octosporus (strain yFS286) (Fission yeast)
OS   (Octosporomyces octosporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=483514 {ECO:0000313|EMBL:EPX71863.1};
RN   [1] {ECO:0000313|EMBL:EPX71863.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YFS286 {ECO:0000313|EMBL:EPX71863.1};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [2] {ECO:0000313|EMBL:EPX71863.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YFS286 {ECO:0000313|EMBL:EPX71863.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Nusbaum C., Russ C., Rhind N., Niki H., Allshire R., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Birren B.;
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KE503207; EPX71863.1; -; Genomic_DNA.
DR   RefSeq; XP_013019163.1; XM_013163709.1.
DR   AlphaFoldDB; S9PWK7; -.
DR   EnsemblFungi; EPX71863; EPX71863; SOCG_03799.
DR   GeneID; 25032767; -.
DR   VEuPathDB; FungiDB:SOCG_03799; -.
DR   eggNOG; KOG0715; Eukaryota.
DR   HOGENOM; CLU_017633_0_3_1; -.
DR   OMA; CPECAGD; -.
DR   OrthoDB; 276132at2759; -.
DR   Proteomes; UP000016088; 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}; 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          79..143
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          219..300
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         219..300
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          445..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  55849 MW;  CD30851948897B74 CRC64;
     MIPFGLRSNI STLHSFASRN TCHRLSKARR NISQPIRRAF ASHALNAKIS YISRNANTAR
     PYRFQRFFHA SNPAFEMTDP YKTLGVSKNA SPKEIKSAYY KLAKQYHPDA NPDKSAQEKF
     VDIKQAYELL QDPEKKKAFD TYGSGAFRNG EFTGNDFGGF QNGFESAFGS GFPGFNFEDL
     FSSFTGRAGR GRRANPFEVY VGEDAEVSLN IDFMEAVKGV KKDVVYSVSS TCSSCHGSGL
     QTGAHRSTCF ACKGSGHRLH FIPPSMHMQS TCDVCGGSGT TIPSSSACRS CSGSGNVRER
     KTISLDIPAG IDDNTVLRVV GAGNDAATAK AAPDAKSRPG DLYATVRVRK HQFFSRQGNN
     VLYRAKVPMT TAALGGTIRI PTLTGEVDLR VPPGTVSGDR ITMTGKGIRN VSGIARYGNF
     YIDFEVNTPK ALSPHERSLL EQLADSLNDT SARRTTPRPT AKDEPPASSD SSSKDKPSES
     SSAGSKSEGS VGGFLKRAFR RLHNEDGSEN ASGNSK
//
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