ID G0HN61_THES4 Unreviewed; 196 AA.
AC G0HN61;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Exosome complex component Csl4 {ECO:0000256|HAMAP-Rule:MF_00975};
GN Name=csl4 {ECO:0000256|HAMAP-Rule:MF_00975};
GN OrderedLocusNames=GQS_03340 {ECO:0000313|EMBL:AEK72569.1};
OS Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK72569.1, ECO:0000313|Proteomes:UP000000874};
RN [1] {ECO:0000313|EMBL:AEK72569.1, ECO:0000313|Proteomes:UP000000874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX PubMed=21914870; DOI=10.1128/JB.05851-11;
RA Wang X., Gao Z., Xu X., Ruan L.;
RT "Complete genome sequence of Thermococcus sp. strain 4557, a
RT hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT area.";
RL J. Bacteriol. 193:5544-5545(2011).
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; CP002920; AEK72569.1; -; Genomic_DNA.
DR RefSeq; WP_014012253.1; NC_015865.1.
DR AlphaFoldDB; G0HN61; -.
DR STRING; 1042877.GQS_03340; -.
DR GeneID; 11015319; -.
DR KEGG; the:GQS_03340; -.
DR PATRIC; fig|1042877.9.peg.651; -.
DR eggNOG; arCOG00676; Archaea.
DR HOGENOM; CLU_067135_1_1_2; -.
DR OrthoDB; 6768at2157; -.
DR Proteomes; UP000000874; 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 Zinc {ECO:0000256|HAMAP-Rule:MF_00975}.
FT DOMAIN 70..149
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
SQ SEQUENCE 196 AA; 21509 MW; D8DBF8A2B9808D9F CRC64;
MDEKNGAKNG DIVLPGDYLG VIEEYFPGEG VKEENGELYA VRAGKVVIDQ DRMEISVEPV
TDTPPLPQVG DVVIANVIEV KPQAAIVQLI KIEGREDDRE IATSKLAGIH ISQVRDGYVE
GMSTEFKVGD IVRARVVATE KSPIQLSTKG PDLGVVYALC SRCRTPLVRR GDKLICPRCG
SVETRKLSTL YRKMRV
//
