JAC1_SCHPO
ID JAC1_SCHPO Reviewed; 225 AA.
AC Q9UTL6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=J-type co-chaperone jac1, mitochondrial {ECO:0000303|PubMed:26545917};
DE AltName: Full=J-type accessory chaperone 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=jac1 {ECO:0000303|PubMed:26545917}; ORFNames=SPAC144.08;
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).
RN [3]
RP FUNCTION, INTERACTION WITH SSC1, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP HIS-98; PRO-99 AND ASP-100.
RX PubMed=26545917; DOI=10.1093/molbev/msv254;
RA Delewski W., Paterkiewicz B., Manicki M., Schilke B., Tomiczek B.,
RA Ciesielski S.J., Nierzwicki L., Czub J., Dutkiewicz R., Craig E.A.,
RA Marszalek J.;
RT "Iron-Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of
RT Mutational Robustness of a Highly Specific Protein-Protein Interaction.";
RL Mol. Biol. Evol. 33:643-656(2016).
CC -!- FUNCTION: Co-chaperone required for the assembly of iron-sulfur (Fe/S)
CC clusters in mitochondria (PubMed:26545917). Stimulates the ATPase
CC activity of the mitochondrial Hsp70 chaperone ssc1, to mediate the
CC transfer of iron-sulfur clusters from isu1 to grx5 (PubMed:26545917).
CC {ECO:0000269|PubMed:26545917}.
CC -!- SUBUNIT: Interacts with ssc1. {ECO:0000269|PubMed:26545917}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Inviable. {ECO:0000269|PubMed:26545917}.
CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
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DR EMBL; CU329670; CAB59688.1; -; Genomic_DNA.
DR PIR; T37675; T37675.
DR RefSeq; NP_594669.1; NM_001020098.2.
DR AlphaFoldDB; Q9UTL6; -.
DR SMR; Q9UTL6; -.
DR STRING; 4896.SPAC144.08.1; -.
DR MaxQB; Q9UTL6; -.
DR PaxDb; Q9UTL6; -.
DR EnsemblFungi; SPAC144.08.1; SPAC144.08.1:pep; SPAC144.08.
DR PomBase; SPAC144.08; jac1.
DR VEuPathDB; FungiDB:SPAC144.08; -.
DR eggNOG; KOG3192; Eukaryota.
DR HOGENOM; CLU_068529_1_1_1; -.
DR InParanoid; Q9UTL6; -.
DR OMA; ECVRLRF; -.
DR PhylomeDB; Q9UTL6; -.
DR Reactome; R-SPO-1268020; Mitochondrial protein import.
DR Reactome; R-SPO-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR PRO; PR:Q9UTL6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0001671; F:ATPase activator activity; IDA:PomBase.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0030544; F:Hsp70 protein binding; ISM:PomBase.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; EXP:PomBase.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.20.1280.20; -; 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 PANTHER; PTHR14021; PTHR14021; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF47144; SSF47144; 1.
DR TIGRFAMs; TIGR00714; hscB; 1.
PE 1: Evidence at protein level;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 50..225
FT /note="J-type co-chaperone jac1, mitochondrial"
FT /id="PRO_0000363388"
FT DOMAIN 61..137
FT /note="J"
FT MOTIF 98..100
FT /note="HSP70 binding"
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 98
FT /note="H->A: Inviable. Abolishes jac1 ATPase activator
FT activity."
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 99
FT /note="P->A: Inviable. Abolishes jac1 ATPase activator
FT activity."
FT /evidence="ECO:0000269|PubMed:26545917"
FT MUTAGEN 100
FT /note="D->A: Inviable. Abolishes jac1 ATPase activator
FT activity."
FT /evidence="ECO:0000269|PubMed:26545917"
SQ SEQUENCE 225 AA; 25901 MW; 41F3DB1FBED9C466 CRC64;
MLKQAGNQSF RPFISFAQKS LFNRQITGNH WIFARFKFYP LNKIVNYNHF HSSSCQSEAK
NFYKQFEGDI SDPPPKGPFD IDLGALKSSY LRKMKTLHPD VAQGKDAALA QRDSAELSKA
YNTLKAPLTR AEYILQLQGI NPVSEDISNS DPEFLMEIMD VHENISASRD SPEKLLQLSQ
ENQGRKVQEI NEIRKAMESS NWDSALLYVN RLRYWNTIDK ILHDL
