CSL4_ARCFU
ID CSL4_ARCFU Reviewed; 179 AA.
AC O30033;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Exosome complex component Csl4 {ECO:0000255|HAMAP-Rule:MF_00975};
GN Name=csl4 {ECO:0000255|HAMAP-Rule:MF_00975}; OrderedLocusNames=AF_0206;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH RRP41; RRP42 AND
RP ZINC, FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=16285927; DOI=10.1016/j.molcel.2005.10.018;
RA Buttner K., Wenig K., Hopfner K.P.;
RT "Structural framework for the mechanism of archaeal exosomes in RNA
RT processing.";
RL Mol. Cell 20:461-471(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH RRP41; RRP42 AND
RP ZINC, FUNCTION, AND SUBUNIT.
RX PubMed=20392821; DOI=10.1093/nar/gkq238;
RA Hartung S., Niederberger T., Hartung M., Tresch A., Hopfner K.P.;
RT "Quantitative analysis of processive RNA degradation by the archaeal RNA
RT exosome.";
RL Nucleic Acids Res. 38:5166-5176(2010).
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 (Probable). {ECO:0000305|PubMed:16285927,
CC ECO:0000305|PubMed:20392821}.
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 (Probable). {ECO:0000305|PubMed:16285927,
CC ECO:0000305|PubMed:20392821}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00975}.
CC -!- DOMAIN: Contains an N-terminal domain that mediates interactions with
CC the hexameric ring, a central S1 domain and a C-terminal zinc-ribbon
CC domain. {ECO:0000269|PubMed:16285927}.
CC -!- MISCELLANEOUS: The zinc ion has probably a structural role.
CC {ECO:0000305|PubMed:16285927}.
CC -!- SIMILARITY: Belongs to the CSL4 family. {ECO:0000255|HAMAP-
CC Rule:MF_00975}.
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DR EMBL; AE000782; AAB91036.1; -; Genomic_DNA.
DR PIR; F69275; F69275.
DR RefSeq; WP_010877717.1; NC_000917.1.
DR PDB; 2BA1; X-ray; 2.70 A; A/B/C=1-179.
DR PDB; 3M7N; X-ray; 2.40 A; A/B/C=1-179.
DR PDB; 3M85; X-ray; 3.00 A; A/B/C=1-179.
DR PDBsum; 2BA1; -.
DR PDBsum; 3M7N; -.
DR PDBsum; 3M85; -.
DR AlphaFoldDB; O30033; -.
DR SMR; O30033; -.
DR STRING; 224325.AF_0206; -.
DR EnsemblBacteria; AAB91036; AAB91036; AF_0206.
DR GeneID; 24793740; -.
DR KEGG; afu:AF_0206; -.
DR eggNOG; arCOG00676; Archaea.
DR HOGENOM; CLU_067135_1_1_2; -.
DR OMA; CGNVETR; -.
DR OrthoDB; 111542at2157; -.
DR PhylomeDB; O30033; -.
DR EvolutionaryTrace; O30033; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA 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; IPR019495; EXOSC1_C.
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 PANTHER; PTHR12686; PTHR12686; 1.
DR Pfam; PF14382; ECR1_N; 1.
DR Pfam; PF10447; EXOSC1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Exosome; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..179
FT /note="Exosome complex component Csl4"
FT /id="PRO_0000424720"
FT DOMAIN 58..137
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00975"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00975,
FT ECO:0000269|PubMed:16285927, ECO:0000269|PubMed:20392821"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00975,
FT ECO:0000269|PubMed:16285927, ECO:0000269|PubMed:20392821"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00975,
FT ECO:0000269|PubMed:16285927, ECO:0000269|PubMed:20392821"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00975,
FT ECO:0000269|PubMed:16285927, ECO:0000269|PubMed:20392821"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:3M7N"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 28..40
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:3M7N"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3M7N"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:3M7N"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3M85"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3M7N"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2BA1"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3M7N"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:3M7N"
SQ SEQUENCE 179 AA; 19597 MW; 3106D5592EF6EAF7 CRC64;
MRFVMPGDRI GSAEEYVKGE GVYEEGGELF AAVAGKLIIK DRVAKVESIS PIPEIVKGDV
VLGRVVDLRN SIALIEVSSK KGENRGPSNR GIGILHVSNV DEGYVKEISE AVGYLDILKA
RVIGDNLRLS TKEEEMGVLR ALCSNCKTEM VREGDILKCP ECGRVEKRKI STDYGKGEW
