ID   C6A1R3_THESM            Unreviewed;       199 AA.
AC   C6A1R3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Exosome complex component Csl4 {ECO:0000256|HAMAP-Rule:MF_00975};
GN   Name=csl4 {ECO:0000256|HAMAP-Rule:MF_00975};
GN   OrderedLocusNames=TSIB_0492 {ECO:0000313|EMBL:ACS89558.1};
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS89558.1, ECO:0000313|Proteomes:UP000009079};
RN   [1] {ECO:0000313|EMBL:ACS89558.1, ECO:0000313|Proteomes:UP000009079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739 {ECO:0000313|Proteomes:UP000009079};
RX   PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
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:0000256|HAMAP-Rule:MF_00975}.
CC   -!- SUBUNIT: Component of the archaeal exosome complex. Forms a trimer of
CC       Rrp4 and/or Csl4 subunits. The trimer associates with an hexameric
CC       ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers. Interacts
CC       with DnaG. {ECO:0000256|HAMAP-Rule:MF_00975}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00975}.
CC       Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- SIMILARITY: Belongs to the CSL4 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00975}.
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DR   EMBL; CP001463; ACS89558.1; -; Genomic_DNA.
DR   RefSeq; WP_015848778.1; NC_012883.1.
DR   AlphaFoldDB; C6A1R3; -.
DR   STRING; 604354.TSIB_0492; -.
DR   GeneID; 8095479; -.
DR   KEGG; tsi:TSIB_0492; -.
DR   eggNOG; arCOG00676; Archaea.
DR   HOGENOM; CLU_067135_1_1_2; -.
DR   OrthoDB; 6768at2157; -.
DR   Proteomes; UP000009079; 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; 2.20.70.10; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR003029; S1_domain.
DR   PANTHER; PTHR12686; 3'-5' EXORIBONUCLEASE CSL4-RELATED; 1.
DR   PANTHER; PTHR12686:SF8; EXOSOME COMPLEX COMPONENT CSL4; 1.
DR   Pfam; PF14382; ECR1_N; 1.
DR   Pfam; PF10447; EXOSC1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF110324; Ribosomal L27 protein-like; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00975};
KW   Exosome {ECO:0000256|ARBA:ARBA00022835, ECO:0000256|HAMAP-Rule:MF_00975};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009079};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00975}.
FT   DOMAIN          72..151
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
SQ   SEQUENCE   199 AA;  21969 MW;  C318B5D843342394 CRC64;
     MVEPKKKTVE NGELVLPGDY LGVIEEFLPG EGVIEENGEL YAARMGRVKI DLEKIEISVE
     PVTDVPPLPQ VGDIVIARVL EVKSQAAIVE LLKIEGRKGY REIATSKLAG IHVSQVKDGY
     VESMNSEFKI GDIVRAKVLT NNKSPIQLTT REPDLGVIYA LCSSCKVSLV RKGNALVCPK
     CGRSESRKLS TYYRKLRLE
//