ID   CNS1_SCHPO              Reviewed;         358 AA.
AC   O13754;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Hsp70/Hsp90 co-chaperone cns1;
GN   Name=cns1; ORFNames=SPAC17A2.04c;
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   -!- FUNCTION: Co-chaperone that binds to the molecular chaperones Hsp90 and
CC       Hsp70. Stimulates Hsp70 ATPase activity, but not Hsp90 ATPase activity.
CC       Involved in only a subset of Hsp90 functions (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Component of Hsp70 and Hsp90 chaperone complexes (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the TTC4 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16559.1; -; Genomic_DNA.
DR   PIR; T37805; T37805.
DR   RefSeq; NP_594238.1; NM_001019661.2.
DR   AlphaFoldDB; O13754; -.
DR   SMR; O13754; -.
DR   BioGRID; 278647; 1.
DR   STRING; 4896.SPAC17A2.04c.1; -.
DR   MaxQB; O13754; -.
DR   PaxDb; O13754; -.
DR   EnsemblFungi; SPAC17A2.04c.1; SPAC17A2.04c.1:pep; SPAC17A2.04c.
DR   GeneID; 2542172; -.
DR   KEGG; spo:SPAC17A2.04c; -.
DR   PomBase; SPAC17A2.04c; cns1.
DR   VEuPathDB; FungiDB:SPAC17A2.04c; -.
DR   eggNOG; KOG0551; Eukaryota.
DR   HOGENOM; CLU_040446_1_0_1; -.
DR   InParanoid; O13754; -.
DR   OMA; HPMFEGL; -.
DR   PhylomeDB; O13754; -.
DR   PRO; PR:O13754; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR   GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR   GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; ISO:PomBase.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR044059; Csn1/TTC4_wheel.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF18972; Wheel; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Nucleus; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..358
FT                   /note="Hsp70/Hsp90 co-chaperone cns1"
FT                   /id="PRO_0000363376"
FT   REPEAT          64..97
FT                   /note="TPR 1"
FT   REPEAT          102..135
FT                   /note="TPR 2"
FT   REPEAT          136..169
FT                   /note="TPR 3"
FT   REPEAT          221..255
FT                   /note="TPR 4"
SQ   SEQUENCE   358 AA;  40531 MW;  E817EE24F1CAF792 CRC64;
     MAGFQSSEVD PNTKNKNAEE MFNELNKVPF FMQSLEDVGD ESENNVQLDA LKALAYEGEP
     HEVAQNFREH GNECFASKRY KDAEEFYTKA LAQKCGDKDI EIACYSNRAA CNLLFENYRQ
     VLNDCAQVLQ RDSTHAKAYY RSAKALVALK RYDEAKECIR LCSLVHPNDP AILALSKELQ
     KKSDDFEKRE SEKKRVAQEK VIAAKTVLLA LQERHIKTKT TEHPPDLGDA MISLSTFDDP
     KSELFFPTIL LYPLVYQSDF VPSVSENCTP LELLKTVFQS PAPWDVHQLY NPDSLDVFAT
     TDTLGLIKVG KNVPILKALT HPKVTLIDGL VQLHVVPHHL ASDWISSWKK NKQENAKN