ID Q6L144_PICTO Unreviewed; 186 AA.
AC Q6L144; A0A8G2FVU0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Exosome complex component Csl4 {ECO:0000256|HAMAP-Rule:MF_00975};
GN Name=csl4 {ECO:0000256|HAMAP-Rule:MF_00975};
GN OrderedLocusNames=PTO0723 {ECO:0000313|EMBL:AAT43308.1};
GN ORFNames=SAMN02745355_0263 {ECO:0000313|EMBL:SMD30384.1};
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828 / KAW 2/3).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=1122961 {ECO:0000313|EMBL:AAT43308.1, ECO:0000313|Proteomes:UP000000438};
RN [1] {ECO:0000313|EMBL:AAT43308.1, ECO:0000313|Proteomes:UP000000438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
RC {ECO:0000313|Proteomes:UP000000438}, and DSM 9790
RC {ECO:0000313|EMBL:AAT43308.1};
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Futterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
RN [2] {ECO:0000313|EMBL:AAT43308.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 9790 {ECO:0000313|EMBL:AAT43308.1};
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SMD30384.1, ECO:0000313|Proteomes:UP000192315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9789 {ECO:0000313|EMBL:SMD30384.1,
RC ECO:0000313|Proteomes:UP000192315};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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; AE017261; AAT43308.1; -; Genomic_DNA.
DR EMBL; FWYE01000001; SMD30384.1; -; Genomic_DNA.
DR RefSeq; WP_011177524.1; NZ_FWYE01000001.1.
DR AlphaFoldDB; Q6L144; -.
DR STRING; 263820.PTO0723; -.
DR PaxDb; 263820-PTO0723; -.
DR GeneID; 2845095; -.
DR KEGG; pto:PTO0723; -.
DR eggNOG; arCOG00676; Archaea.
DR HOGENOM; CLU_067135_1_1_2; -.
DR InParanoid; Q6L144; -.
DR OrthoDB; 6768at2157; -.
DR Proteomes; UP000000438; Chromosome.
DR Proteomes; UP000192315; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
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 PANTHER; PTHR12686; 3'-5' EXORIBONUCLEASE CSL4-RELATED; 1.
DR PANTHER; PTHR12686:SF8; EXOSOME COMPLEX COMPONENT CSL4; 1.
DR Pfam; PF14382; ECR1_N; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF110324; Ribosomal L27 protein-like; 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:UP000192315};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00975}.
FT DOMAIN 8..41
FT /note="Exosome complex component N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14382"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
SQ SEQUENCE 186 AA; 21099 MW; 055EA73753E7270C CRC64;
MHGSISYPGD VIASEEEYLP GKNTIEDAGN IISLCYGEVV KDDRNLVISV RPMKHERALK
VGDIVYGMVL KVTNNEATVH IYAVEDNRLI PVEKDAKLRL PILNRNYTQM VSLGDMLRGK
VLTTKPLYIT IFSTHLGVLR TRCTVCRREM VIKNNVLYCT NCKRIERRKI SDDYGNINIG
DNNEGR
//
