XDJ1_YEAST
ID XDJ1_YEAST Reviewed; 459 AA.
AC P39102; D6VY90; Q12014;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=DnaJ protein homolog XDJ1;
GN Name=XDJ1; OrderedLocusNames=YLR090W; ORFNames=L9449.3;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24657 / D273-10B;
RX PubMed=8045410; DOI=10.1016/0378-1119(94)90333-6;
RA Schwarz E., Westermann B., Caplan A.J., Ludwig G., Neupert W.;
RT "XDJ1, a gene encoding a novel non-essential DnaJ homologue from
RT Saccharomyces cerevisiae.";
RL Gene 145:121-124(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16689936; DOI=10.1111/j.1742-4658.2006.05171.x;
RA Burri L., Vascotto K., Gentle I.E., Chan N.C., Beilharz T., Stapleton D.I.,
RA Ramage L., Lithgow T.;
RT "Integral membrane proteins in the mitochondrial outer membrane of
RT Saccharomyces cerevisiae.";
RL FEBS J. 273:1507-1515(2006).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16689936,
CC ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 1210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X76343; CAA53962.1; -; Genomic_DNA.
DR EMBL; U53880; AAB67594.1; -; Genomic_DNA.
DR EMBL; Z73262; CAA97651.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09406.1; -; Genomic_DNA.
DR PIR; S64924; S64924.
DR RefSeq; NP_013191.1; NM_001181977.1.
DR AlphaFoldDB; P39102; -.
DR SMR; P39102; -.
DR BioGRID; 31363; 161.
DR DIP; DIP-990N; -.
DR IntAct; P39102; 4.
DR MINT; P39102; -.
DR STRING; 4932.YLR090W; -.
DR iPTMnet; P39102; -.
DR MaxQB; P39102; -.
DR PaxDb; P39102; -.
DR PRIDE; P39102; -.
DR EnsemblFungi; YLR090W_mRNA; YLR090W; YLR090W.
DR GeneID; 850779; -.
DR KEGG; sce:YLR090W; -.
DR SGD; S000004080; XDJ1.
DR VEuPathDB; FungiDB:YLR090W; -.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; P39102; -.
DR OMA; YKRQKLC; -.
DR BioCyc; YEAST:G3O-32240-MON; -.
DR PRO; PR:P39102; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P39102; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 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; ISS:SGD.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR044713; DNJA1/2-like.
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; PTHR43888; PTHR43888; 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; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW Chaperone; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..459
FT /note="DnaJ protein homolog XDJ1"
FT /id="PRO_0000071121"
FT DOMAIN 7..79
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REPEAT 159..166
FT /note="CXXCXGXG motif"
FT REPEAT 181..188
FT /note="CXXCXGXG motif"
FT REPEAT 208..215
FT /note="CXXCXGXG motif"
FT REPEAT 228..235
FT /note="CXXCXGXG motif"
FT ZN_FING 146..240
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT CONFLICT 119
FT /note="D -> E (in Ref. 1; CAA53962)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="H -> Y (in Ref. 1; CAA53962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 51347 MW; 1C459F9947F33A44 CRC64;
MSGSDRGDRL YDVLGVTRDA TVQEIKTAYR KLALKHHPDK YVDQDSKEVN EIKFKEITAA
YEILSDPEKK SHYDLYGDDN GAASSGGANG FGDEDFMNFF NNFFNNGSHD GNNFPGEYDA
YEEGNSTSSK DIDIDISLTL KDLYMGKKLK FDLKRQVICI KCHGSGWKPK RKIHVTHDVE
CESCAGKGSK ERLKRFGPGL VASQWVVCEK CNGKGKYTKR PKNPKNFCPD CAGLGLLSKK
EIITVNVAPG HHFNDVITVK GMADEEIDKT TCGDLKFHLT EKQENLEQKQ IFLKNFDDGA
GEDLYTSITI SLSEALTGFE KFLTKTFDDR LLTLSVKPGR VVRPGDTIKI ANEGWPILDN
PHGRCGDLYV FVHIEFPPDN WFNEKSELLA IKTNLPSSSS CASHATVNTE DDSNLTNNET
ISNFRIIHTD DLPEGIRPFK PEAQDSAHQK ARSSYCCIQ
