XDJ1_SCHPO
ID XDJ1_SCHPO Reviewed; 413 AA.
AC O94657;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DnaJ protein homolog xdj1;
DE Flags: Precursor;
GN Name=xdj1; ORFNames=SPBC405.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Lipid-anchor {ECO:0000305}.
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DR EMBL; CU329671; CAB38605.1; -; Genomic_DNA.
DR PIR; T40427; T40427.
DR RefSeq; NP_596309.1; NM_001022231.2.
DR AlphaFoldDB; O94657; -.
DR SMR; O94657; -.
DR BioGRID; 277293; 3.
DR STRING; 4896.SPBC405.06.1; -.
DR iPTMnet; O94657; -.
DR MaxQB; O94657; -.
DR PaxDb; O94657; -.
DR PRIDE; O94657; -.
DR EnsemblFungi; SPBC405.06.1; SPBC405.06.1:pep; SPBC405.06.
DR GeneID; 2540773; -.
DR KEGG; spo:SPBC405.06; -.
DR PomBase; SPBC405.06; xdj1.
DR VEuPathDB; FungiDB:SPBC405.06; -.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; O94657; -.
DR OMA; GMSAFNG; -.
DR PhylomeDB; O94657; -.
DR PRO; PR:O94657; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0005634; C:nucleus; ISS:PomBase.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 protein binding; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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 3: Inferred from homology;
KW Chaperone; Endoplasmic reticulum; Lipoprotein; Membrane; Metal-binding;
KW Methylation; Prenylation; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..410
FT /note="DnaJ protein homolog xdj1"
FT /id="PRO_0000314108"
FT PROPEP 411..413
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396659"
FT DOMAIN 6..73
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REPEAT 147..154
FT /note="CXXCXGXG motif"
FT REPEAT 164..171
FT /note="CXXCXGXG motif"
FT REPEAT 191..198
FT /note="CXXCXGXG motif"
FT REPEAT 207..214
FT /note="CXXCXGXG motif"
FT ZN_FING 134..219
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT MOD_RES 410
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 410
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 413 AA; 46126 MW; BD6F29E458591D6A CRC64;
MVVDTKLYDI LEVHFEASAE EIKKSYKRLA LLHHPDKAPI HEKEEAAERF RGVQEAYDIL
KDPESREMYD MYGMNSDSNS QFDGGVNLDD VLAQMFGMNF EAGGPGKNVP RDRKRRGSDV
IHDYEISLED MFKGKEVKLR ATRNTLCPRC QGRGGKRFAK EKPCLSCDGK GVKQHLKHVG
PHHVTNSQVI CDTCNGKGVS FRGKDRCKHC KGSGTVPEQR MLSFFVNRSA KENDKIIQRG
MADEAYGITP GDVILQLHQK PHPVFERLGD DLKAKLKISL AEALTGFNRV ILTTLDGRGL
EYVQPIGKIL HPGDCLIIPG EGMYKDSKTD LRGDLYLEVD IEFPKDGLIG TTEIEILRDI
LPSIPKVSVM DDTLIDSVRG VPGDISHFGG DARYANEDYG DETYEGVPEC QAQ
