ZUO1_SCHPO
ID ZUO1_SCHPO Reviewed; 442 AA.
AC Q9Y7I8; O14347;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Zuotin;
DE AltName: Full=DnaJ-related protein zuo1;
DE Short=J protein zuo1;
DE AltName: Full=Ribosome-associated complex subunit zuo1;
GN Name=zuo1; ORFNames=SPBC1778.01c, SPBC30D10.01;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55; SER-57 AND SER-76, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Component of the ribosome-associated complex (RAC), a
CC heterodimeric chaperone complex involved in regulation of accurate
CC translation termination and in folding or maintaining nascent
CC polypeptides in a folding-competent state. RAC stimulates the ATPase
CC activity of the ribosome-associated pool of Hsp70-type chaperones
CC SSB1/SSB2 that bind to the nascent polypeptide chain (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: RAC is a heterodimer of the Hsp70/DnaK-type chaperone ssz1 and
CC the Hsp40/DnaJ-type chaperone zuo1. RAC associates with ribosomes via
CC zuo1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB10796.1; -; Genomic_DNA.
DR PIR; T39683; T39683.
DR RefSeq; NP_596284.2; NM_001022205.3.
DR AlphaFoldDB; Q9Y7I8; -.
DR SMR; Q9Y7I8; -.
DR BioGRID; 276351; 3.
DR STRING; 4896.SPBC1778.01c.1; -.
DR iPTMnet; Q9Y7I8; -.
DR MaxQB; Q9Y7I8; -.
DR PaxDb; Q9Y7I8; -.
DR PRIDE; Q9Y7I8; -.
DR EnsemblFungi; SPBC1778.01c.1; SPBC1778.01c.1:pep; SPBC1778.01c.
DR GeneID; 2539801; -.
DR KEGG; spo:SPBC1778.01c; -.
DR PomBase; SPBC1778.01c; zuo1.
DR VEuPathDB; FungiDB:SPBC1778.01c; -.
DR eggNOG; KOG0724; Eukaryota.
DR HOGENOM; CLU_019916_1_0_1; -.
DR InParanoid; Q9Y7I8; -.
DR OMA; SNRDHKR; -.
DR PhylomeDB; Q9Y7I8; -.
DR PRO; PR:Q9Y7I8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030544; F:Hsp70 protein binding; ISM:PomBase.
DR GO; GO:0043022; F:ribosome binding; ISO:PomBase.
DR GO; GO:0051082; F:unfolded protein binding; ISO:PomBase.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; ISO:PomBase.
DR GO; GO:0002182; P:cytoplasmic translational elongation; NAS:PomBase.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.10.8.840; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR032003; RAC_head.
DR InterPro; IPR042569; RAC_head_sf.
DR InterPro; IPR044634; Zuotin/DnaJC2.
DR PANTHER; PTHR43999; PTHR43999; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF16717; RAC_head; 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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..442
FT /note="Zuotin"
FT /id="PRO_0000071159"
FT DOMAIN 97..167
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 49..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 442 AA; 50209 MW; F4EC924871B7318B CRC64;
MSAGDSIQLF PPTTKQAIEA SFVPHGKISP LIKRAVEPVG PLFLAHARRQ RHGRTFSEDE
RLEVKNKVQE EVKEESEDEE EDPAMLRADP KEWKQQDHYA VLGLSKYRYK ADTEQIKKAH
LKKVLKHHPD KKAASGNIND DSFFKCIQKA YEILSDPVRR RQFDSVDENA DVEPPESTTK
ETFFELWTPV FESEARFSKK QPVPSLGTIE STRAEVDNFY NFWYNFDSWR SFEYLDKDIP
DDGESRDNKR FQEKKNRSER QKNKARDNAR LRNLVDTALA SDPRIKLFKE QEKAAKAARK
WEREAGAREA AAAAQKKKEE EERRAAEEAA AKASAAAANK KAKEDKKKAQ KRDKKVVKNA
LKDFNYFSAT DVPSAEHVDS VLKDVDVIMS KLGEGELGQL AADINAEKAA GAASVQAVFD
KFAKMFIERG SMSSADVVFF AQ
