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Exosome complex component Csl4

 CSL4_SULSO              Reviewed;         189 AA.
Q980J9;
11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 1.
20-JUN-2018, entry version 78.
RecName: Full=Exosome complex component Csl4 {ECO:0000255|HAMAP-Rule:MF_00975};
Name=csl4 {ECO:0000255|HAMAP-Rule:MF_00975};
OrderedLocusNames=SSO0292;
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 /
P2).
Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
Sulfolobus.
NCBI_TaxID=273057;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=11427726; DOI=10.1073/pnas.141222098;
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G.,
Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
"The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
[2]
INTERACTION WITH EXOSOME.
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=12947419; DOI=10.1038/sj.embor.embor929;
Evguenieva-Hackenberg E., Walter P., Hochleitner E., Lottspeich F.,
Klug G.;
"An exosome-like complex in Sulfolobus solfataricus.";
EMBO Rep. 4:889-893(2003).
[3]
FUNCTION, AND INTERACTION WITH EXOSOME.
PubMed=17078816; DOI=10.1111/j.1365-2958.2006.05393.x;
Walter P., Klein F., Lorentzen E., Ilchmann A., Klug G.,
Evguenieva-Hackenberg E.;
"Characterization of native and reconstituted exosome complexes from
the hyperthermophilic archaeon Sulfolobus solfataricus.";
Mol. Microbiol. 62:1076-1089(2006).
[4]
FUNCTION.
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=19053279; DOI=10.1021/bi8012214;
Evguenieva-Hackenberg E., Roppelt V., Finsterseifer P., Klug G.;
"Rrp4 and Csl4 are needed for efficient degradation but not for
polyadenylation of synthetic and natural RNA by the archaeal
exosome.";
Biochemistry 47:13158-13168(2008).
[5]
FUNCTION.
PubMed=20488184; DOI=10.1016/j.febslet.2010.05.014;
Roppelt V., Klug G., Evguenieva-Hackenberg E.;
"The evolutionarily conserved subunits Rrp4 and Csl4 confer different
substrate specificities to the archaeal exosome.";
FEBS Lett. 584:2931-2936(2010).
[6]
SUBUNIT.
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=22503705; DOI=10.1016/j.biochi.2012.03.026;
Witharana C., Roppelt V., Lochnit G., Klug G.,
Evguenieva-Hackenberg E.;
"Heterogeneous complexes of the RNA exosome in Sulfolobus
solfataricus.";
Biochimie 94:1578-1587(2012).
[7]
INTERACTION WITH DNAG.
PubMed=23324612; DOI=10.4161/rna.23450;
Hou L., Klug G., Evguenieva-Hackenberg E.;
"The archaeal DnaG protein needs Csl4 for binding to the exosome and
enhances its interaction with adenine-rich RNAs.";
RNA Biol. 10:415-424(2013).
-!- FUNCTION: Non-catalytic component of the exosome, which is a
complex involved in RNA degradation. Increases the RNA binding and
the efficiency of RNA degradation. Helpful for the interaction of
the exosome with A-poor RNAs. {ECO:0000255|HAMAP-Rule:MF_00975,
ECO:0000269|PubMed:17078816, ECO:0000269|PubMed:19053279,
ECO:0000269|PubMed:20488184}.
-!- SUBUNIT: Component of the archaeal exosome complex. Forms a trimer
of Rrp4 and/or Csl4 subunits. The trimer associates with a
hexameric ring-like arrangement composed of 3 Rrp41-Rrp42
heterodimers. Interacts with DnaG. {ECO:0000255|HAMAP-
Rule:MF_00975, ECO:0000269|PubMed:12947419,
ECO:0000269|PubMed:17078816, ECO:0000269|PubMed:22503705,
ECO:0000269|PubMed:23324612}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00975}.
-!- SIMILARITY: Belongs to the CSL4 family. {ECO:0000255|HAMAP-
Rule:MF_00975}.
-----------------------------------------------------------------------
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EMBL; AE006641; AAK40632.1; -; Genomic_DNA.
PIR; A90172; A90172.
RefSeq; WP_009990582.1; NC_002754.1.
ProteinModelPortal; Q980J9; -.
STRING; 273057.SSO0292; -.
EnsemblBacteria; AAK40632; AAK40632; SSO0292.
GeneID; 27426589; -.
KEGG; sso:SSO0292; -.
PATRIC; fig|273057.12.peg.287; -.
eggNOG; arCOG00676; Archaea.
eggNOG; COG1096; LUCA.
HOGENOM; HOG000222781; -.
InParanoid; Q980J9; -.
KO; K07573; -.
OMA; CGNVETR; -.
OrthoDB; POG093Z0LVA; -.
Proteomes; UP000001974; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0006396; P:RNA processing; IEA:InterPro.
HAMAP; MF_00975; Exosome_Csl4; 1.
InterPro; IPR025721; Exosome_cplx_N_dom.
InterPro; IPR030850; Exosome_Csl4_arc.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR022967; S1_dom.
InterPro; IPR003029; S1_domain.
Pfam; PF14382; ECR1_N; 1.
Pfam; PF00575; S1; 1.
SMART; SM00316; S1; 1.
SUPFAM; SSF50249; SSF50249; 1.
PROSITE; PS50126; S1; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Exosome; Metal-binding;
Reference proteome; Zinc.
CHAIN 1 189 Exosome complex component Csl4.
/FTId=PRO_0000424721.
DOMAIN 66 142 S1 motif. {ECO:0000255|HAMAP-
Rule:MF_00975}.
METAL 151 151 Zinc. {ECO:0000255|HAMAP-Rule:MF_00975}.
METAL 154 154 Zinc. {ECO:0000255|HAMAP-Rule:MF_00975}.
METAL 168 168 Zinc. {ECO:0000255|HAMAP-Rule:MF_00975}.
METAL 171 171 Zinc. {ECO:0000255|HAMAP-Rule:MF_00975}.
SEQUENCE 189 AA; 21004 MW; A0D53D88B49E6FDB CRC64;
MRTQGELTLP GEELAVIEEF MTGDGTYEQN GIVRAAVVGK IFYDMLNRKS NVLGFKKIIF
QHLKKAKYVI GIVNSIKEDS ALVSIVGIEE RGLASPISAY LHISQISNKK INNVTDAIKI
GDVIKAKLLS YTFPLALTIK MKDLGVIYAR CSRCGYLLIK QDENNLKCQR CGNIEQRKIG
SYMVKKGGN


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