ID G0V5J1_NAUCC Unreviewed; 188 AA.
AC G0V5J1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 13-SEP-2023, entry version 50.
DE RecName: Full=J domain-containing protein {ECO:0000259|PROSITE:PS50076};
GN Name=NCAS0A01690 {ECO:0000313|EMBL:CCC66727.1};
GN OrderedLocusNames=NCAS_0A01690 {ECO:0000313|EMBL:CCC66727.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC66727.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC66727.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HscB family.
CC {ECO:0000256|ARBA:ARBA00010476}.
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DR EMBL; HE576752; CCC66727.1; -; Genomic_DNA.
DR RefSeq; XP_003673120.1; XM_003673072.1.
DR AlphaFoldDB; G0V5J1; -.
DR STRING; 1064592.G0V5J1; -.
DR GeneID; 11529645; -.
DR KEGG; ncs:NCAS_0A01690; -.
DR eggNOG; KOG3192; Eukaryota.
DR HOGENOM; CLU_068529_1_1_1; -.
DR InParanoid; G0V5J1; -.
DR OMA; TVELKYW; -.
DR OrthoDB; 1479333at2759; -.
DR Proteomes; UP000001640; Chromosome 1.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR004640; HscB.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR009073; HscB_oligo_C.
DR InterPro; IPR036869; J_dom_sf.
DR NCBIfam; TIGR00714; hscB; 1.
DR PANTHER; PTHR14021; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR PANTHER; PTHR14021:SF15; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640}.
FT DOMAIN 13..85
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 188 AA; 22311 MW; E67D587866C96E1D CRC64;
MKRFLTQKRY LTTFYELFPR TFPTKTPIWS VDQSKLRKEY RALQAQHHPD MAQNSEELDT
HSSLLNKAYH VLKEPLTRSQ YLIKLLDNVD LTQDSVKEKI TQSDPEILMK VIEIHEQLMD
IDTEEDVKKI RRENTERMAT IEGQLENAFK KKDFETAIKL TVELKYWSNV AYAIKEWAPG
KEIQINNH
//
