CSL4_SACS2
ID CSL4_SACS2 Reviewed; 189 AA.
AC Q980J9;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Exosome complex component Csl4 {ECO:0000255|HAMAP-Rule:MF_00975};
GN Name=csl4 {ECO:0000255|HAMAP-Rule:MF_00975}; OrderedLocusNames=SSO0292;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP INTERACTION WITH EXOSOME.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=12947419; DOI=10.1038/sj.embor.embor929;
RA Evguenieva-Hackenberg E., Walter P., Hochleitner E., Lottspeich F.,
RA Klug G.;
RT "An exosome-like complex in Sulfolobus solfataricus.";
RL EMBO Rep. 4:889-893(2003).
RN [3]
RP FUNCTION, AND INTERACTION WITH EXOSOME.
RX PubMed=17078816; DOI=10.1111/j.1365-2958.2006.05393.x;
RA Walter P., Klein F., Lorentzen E., Ilchmann A., Klug G.,
RA Evguenieva-Hackenberg E.;
RT "Characterization of native and reconstituted exosome complexes from the
RT hyperthermophilic archaeon Sulfolobus solfataricus.";
RL Mol. Microbiol. 62:1076-1089(2006).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=19053279; DOI=10.1021/bi8012214;
RA Evguenieva-Hackenberg E., Roppelt V., Finsterseifer P., Klug G.;
RT "Rrp4 and Csl4 are needed for efficient degradation but not for
RT polyadenylation of synthetic and natural RNA by the archaeal exosome.";
RL Biochemistry 47:13158-13168(2008).
RN [5]
RP FUNCTION.
RX PubMed=20488184; DOI=10.1016/j.febslet.2010.05.014;
RA Roppelt V., Klug G., Evguenieva-Hackenberg E.;
RT "The evolutionarily conserved subunits Rrp4 and Csl4 confer different
RT substrate specificities to the archaeal exosome.";
RL FEBS Lett. 584:2931-2936(2010).
RN [6]
RP SUBUNIT.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=22503705; DOI=10.1016/j.biochi.2012.03.026;
RA Witharana C., Roppelt V., Lochnit G., Klug G., Evguenieva-Hackenberg E.;
RT "Heterogeneous complexes of the RNA exosome in Sulfolobus solfataricus.";
RL Biochimie 94:1578-1587(2012).
RN [7]
RP INTERACTION WITH DNAG.
RX PubMed=23324612; DOI=10.4161/rna.23450;
RA Hou L., Klug G., Evguenieva-Hackenberg E.;
RT "The archaeal DnaG protein needs Csl4 for binding to the exosome and
RT enhances its interaction with adenine-rich RNAs.";
RL RNA Biol. 10:415-424(2013).
CC -!- FUNCTION: Non-catalytic component of the exosome, which is a complex
CC involved in RNA degradation. Increases the RNA binding and the
CC efficiency of RNA degradation. Helpful for the interaction of the
CC exosome with A-poor RNAs. {ECO:0000255|HAMAP-Rule:MF_00975,
CC ECO:0000269|PubMed:17078816, ECO:0000269|PubMed:19053279,
CC ECO:0000269|PubMed:20488184}.
CC -!- SUBUNIT: Component of the archaeal exosome complex. Forms a trimer of
CC Rrp4 and/or Csl4 subunits. The trimer associates with a hexameric ring-
CC like arrangement composed of 3 Rrp41-Rrp42 heterodimers. Interacts with
CC DnaG. {ECO:0000255|HAMAP-Rule:MF_00975, ECO:0000269|PubMed:12947419,
CC ECO:0000269|PubMed:17078816, ECO:0000269|PubMed:22503705,
CC ECO:0000269|PubMed:23324612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00975}.
CC -!- SIMILARITY: Belongs to the CSL4 family. {ECO:0000255|HAMAP-
CC Rule:MF_00975}.
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DR EMBL; AE006641; AAK40632.1; -; Genomic_DNA.
DR PIR; A90172; A90172.
DR RefSeq; WP_009990582.1; NC_002754.1.
DR AlphaFoldDB; Q980J9; -.
DR SMR; Q980J9; -.
DR STRING; 273057.SSO0292; -.
DR EnsemblBacteria; AAK40632; AAK40632; SSO0292.
DR GeneID; 44129267; -.
DR KEGG; sso:SSO0292; -.
DR PATRIC; fig|273057.12.peg.287; -.
DR eggNOG; arCOG00676; Archaea.
DR HOGENOM; CLU_067135_1_1_2; -.
DR InParanoid; Q980J9; -.
DR OMA; CGNVETR; -.
DR PhylomeDB; Q980J9; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00975; Exosome_Csl4; 1.
DR InterPro; IPR039771; Csl4.
DR InterPro; IPR025721; Exosome_cplx_N_dom.
DR InterPro; IPR030850; Exosome_Csl4_arc.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR12686; PTHR12686; 1.
DR Pfam; PF14382; ECR1_N; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Exosome; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..189
FT /note="Exosome complex component Csl4"
FT /id="PRO_0000424721"
FT DOMAIN 66..142
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00975"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00975"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00975"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00975"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00975"
SQ 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
