ID   RRP4_METS3              Reviewed;         298 AA.
AC   A5UJS0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Exosome complex component Rrp4 {ECO:0000255|HAMAP-Rule:MF_00623};
GN   Name=rrp4 {ECO:0000255|HAMAP-Rule:MF_00623}; OrderedLocusNames=Msm_0243;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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. Confers strong poly(A) specificity to
CC       the exosome. {ECO:0000255|HAMAP-Rule:MF_00623}.
CC   -!- SUBUNIT: Component of the archaeal exosome complex. Forms a trimer of
CC       Rrp4 and/or Csl4 subunits. The trimer associates with a hexameric ring-
CC       like arrangement composed of 3 Rrp41-Rrp42 heterodimers.
CC       {ECO:0000255|HAMAP-Rule:MF_00623}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00623}.
CC   -!- SIMILARITY: Belongs to the RRP4 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00623}.
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; CP000678; ABQ86448.1; -; Genomic_DNA.
DR   RefSeq; WP_011953778.1; NC_009515.1.
DR   AlphaFoldDB; A5UJS0; -.
DR   SMR; A5UJS0; -.
DR   STRING; 420247.Msm_0243; -.
DR   EnsemblBacteria; ABQ86448; ABQ86448; Msm_0243.
DR   GeneID; 5216607; -.
DR   KEGG; msi:Msm_0243; -.
DR   PATRIC; fig|420247.28.peg.246; -.
DR   eggNOG; arCOG00678; Archaea.
DR   HOGENOM; CLU_071769_0_0_2; -.
DR   OMA; GPYIPEV; -.
DR   Proteomes; UP000001992; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR   GO; GO:0008143; F:poly(A) binding; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1370.10; -; 1.
DR   HAMAP; MF_00623; Exosome_Rrp4; 1.
DR   InterPro; IPR025721; Exosome_cplx_N_dom.
DR   InterPro; IPR026699; Exosome_RNA_bind1/RRP40/RRP4.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR023474; Rrp4.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR21321; PTHR21321; 1.
DR   Pfam; PF14382; ECR1_N; 1.
DR   Pfam; PF15985; KH_6; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exosome; RNA-binding.
FT   CHAIN           1..298
FT                   /note="Exosome complex component Rrp4"
FT                   /id="PRO_1000061382"
FT   DOMAIN          63..131
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT   DOMAIN          139..197
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT   REGION          276..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   298 AA;  33843 MW;  B47B5E4C280056DF CRC64;
     MIYVENKDLV IPGEVLADDE YYSGRGTFKE NGKICSSLMG LVSLRNKKIR VIPLKSKYVP
     KKGDVVIGKI KDVRFSMWDV DINSPYSGIL PAFEVFGREK KELNKVFDVG DVLFLRVVDV
     DEVKKVKLGL KGRGMGKFRG GIIVDITPTK VPRLIGKKGS MINMIKDKTN CKIIVGQNGL
     VWVKGEEDME QLTKDIIHMI EAEAHTSGLT NKVKNKLSLA IDGELPQEDD YSDDYEELEK
     PKLQNFKEEL EQEEKEEQSK KDSTDFYKVI EELKKKNKKD KPLSYGNNSG NSYILNNR