ID   E0SNR8_IGNAA            Unreviewed;       187 AA.
AC   E0SNR8;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Exosome complex component Csl4 {ECO:0000256|HAMAP-Rule:MF_00975};
GN   Name=csl4 {ECO:0000256|HAMAP-Rule:MF_00975};
GN   OrderedLocusNames=Igag_1050 {ECO:0000313|EMBL:ADM27864.1};
OS   Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignisphaera.
OX   NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM27864.1, ECO:0000313|Proteomes:UP000001304};
RN   [1] {ECO:0000313|EMBL:ADM27864.1, ECO:0000313|Proteomes:UP000001304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17230 / JCM 13409 / AQ1.S1
RC   {ECO:0000313|Proteomes:UP000001304};
RX   PubMed=21304693; DOI=10.4056/sigs.1072907;
RA   Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Tapia R., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Brambilla E., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Sikorski J.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).";
RL   Stand. Genomic Sci. 3:66-75(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. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002098; ADM27864.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0SNR8; -.
DR   STRING; 583356.Igag_1050; -.
DR   KEGG; iag:Igag_1050; -.
DR   HOGENOM; CLU_067135_1_1_2; -.
DR   Proteomes; UP000001304; 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; 2.20.70.10; -; 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; 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   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|HAMAP-Rule:MF_00975};
KW   Exosome {ECO:0000256|HAMAP-Rule:MF_00975};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001304};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00975}.
FT   DOMAIN          65..130
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
SQ   SEQUENCE   187 AA;  20913 MW;  D04A01ADCF2B0A22 CRC64;
     MSLPPNSIVL PGEKLCVEEE YMPSIGTYSE EGIVRAAIIG RVQYDIINRR IYIKSIKSPV
     IPKAGDIVIG VVEQMRDELA TINIIGYDTN NLFKHSFTGI LHISQASETR IPTLYDVIRV
     GDIIRAKVLN NYIPILLSIK EPRLGVIQAY CSRCGSPLIK SGDKLRCSFC GNIENRKIAF
     DYILRGK
//