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Database: UniProt
Entry: L0L295_METHD
LinkDB: L0L295_METHD
Original site: L0L295_METHD 
ID   L0L295_METHD            Unreviewed;       242 AA.
AC   L0L295;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Exosome complex component Csl4 {ECO:0000256|HAMAP-Rule:MF_00975};
GN   Name=csl4 {ECO:0000256|HAMAP-Rule:MF_00975};
GN   OrderedLocusNames=Metho_2237 {ECO:0000313|EMBL:AGB50399.1};
OS   Methanomethylovorans hollandica (strain DSM 15978 / NBRC 107637 / DMS1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanomethylovorans.
OX   NCBI_TaxID=867904 {ECO:0000313|EMBL:AGB50399.1, ECO:0000313|Proteomes:UP000010866};
RN   [1] {ECO:0000313|Proteomes:UP000010866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15978 / NBRC 107637 / DMS1
RC   {ECO:0000313|Proteomes:UP000010866};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Methanomethylovorans hollandica DSM
RT   15978.";
RL   Submitted (FEB-2012) 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; CP003362; AGB50399.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0L295; -.
DR   STRING; 867904.Metho_2237; -.
DR   KEGG; mhz:Metho_2237; -.
DR   HOGENOM; CLU_067135_1_0_2; -.
DR   Proteomes; UP000010866; 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   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:UP000010866};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00975}.
FT   DOMAIN          119..197
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
FT   BINDING         225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00975"
SQ   SEQUENCE   242 AA;  26363 MW;  0CEE7EAE46BCC854 CRC64;
     MIKGSGEGSE SAQSSEEIEQ KMTKGTKVEA AKVAKVPKRS ITKPPKKVIE EENMDEGELV
     FVMPGDIIGT TEEFIPGIGT FLNVADIHAA STGIVKIDRK ARMISVVPST KYPPSVNVGD
     IVVGSITSLR ESVVLVEIAA IKDEGEREFQ KVGIAAIHVS NVKDSYCKRL DEEFSVGDII
     KAKVLNTENM RLSTAEQELG VMKAQCFNCR TVMVKDNNKL LCPECGRTEK RKLSQDYGTG
     IV
//
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