ID   JJJ2_ASHGO              Reviewed;         535 AA.
AC   Q757X4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=J protein JJJ2;
GN   Name=JJJ2; OrderedLocusNames=AEL112C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR   EMBL; AE016818; AAS52573.1; -; Genomic_DNA.
DR   RefSeq; NP_984749.1; NM_210103.1.
DR   AlphaFoldDB; Q757X4; -.
DR   SMR; Q757X4; -.
DR   STRING; 33169.AAS52573; -.
DR   EnsemblFungi; AAS52573; AAS52573; AGOS_AEL112C.
DR   GeneID; 4620936; -.
DR   KEGG; ago:AGOS_AEL112C; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   HOGENOM; CLU_490950_0_0_1; -.
DR   InParanoid; Q757X4; -.
DR   OMA; ARSKFEC; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR   GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   3: Inferred from homology;
KW   Chaperone; Coiled coil; Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..535
FT                   /note="J protein JJJ2"
FT                   /id="PRO_0000333575"
FT   DOMAIN          12..76
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          87..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          446..499
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        138..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   535 AA;  59682 MW;  2D12A1A2485974B0 CRC64;
     METARIRLDE TTYYSLLGLP FGASELHIRK AYMRLARELH PDKSKSKEAA ELFKVVAHAH
     SVLTDKEKRL KYDRQLIAKG LHTYVSNSSS SLNYKPPGSR PVTRAQQAAV AADKERAAKK
     AKPYEEQPYG FGTEAESSPQ AGDGTPQRST TATKPFKAKS YQHQRNPGTP PETGNKKSST
     FSARFISNSV PAAPESKPSD EYPAKKMPRK QATPEPSSSP FLSPDHRHYA RTKFESRRRG
     TRSASPLKTM PTSQTDTLDG LKSIINKFSD RVKVNIFGSP STVETEHVTD LSEDQSSVEQ
     DGGDEARLRA DMLAGDKATA RCAPIPQDGT KEINLEELNT SLPPQRETFN MRNVSDTLDR
     MNVKRQKLNT EATHVPGNIP LPAQRHLSPA LDESGSLAEP VNKSIPRVYK IDRIPPTEFA
     MDLSVSDIEL PTMPSFHCNI LDKSDIKLCR EKILEFNTKA NRLKKQLIQA LSLRSSADEA
     LENRVVRVEN MAAYVEAKNY DLDVVMKLHE IQNRQRIVAE SFTNLMRSAY ASGTF