ID   RRP4_METBU              Reviewed;         263 AA.
AC   Q12ZB8;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Exosome complex component Rrp4 {ECO:0000255|HAMAP-Rule:MF_00623};
GN   Name=rrp4 {ECO:0000255|HAMAP-Rule:MF_00623}; OrderedLocusNames=Mbur_0198;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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}.
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DR   EMBL; CP000300; ABE51208.1; -; Genomic_DNA.
DR   RefSeq; WP_011498370.1; NC_007955.1.
DR   AlphaFoldDB; Q12ZB8; -.
DR   SMR; Q12ZB8; -.
DR   STRING; 259564.Mbur_0198; -.
DR   EnsemblBacteria; ABE51208; ABE51208; Mbur_0198.
DR   GeneID; 3997165; -.
DR   KEGG; mbu:Mbur_0198; -.
DR   HOGENOM; CLU_071769_0_0_2; -.
DR   OMA; GPYIPEV; -.
DR   OrthoDB; 93052at2157; -.
DR   Proteomes; UP000001979; 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; Reference proteome; RNA-binding.
FT   CHAIN           1..263
FT                   /note="Exosome complex component Rrp4"
FT                   /id="PRO_0000416231"
FT   DOMAIN          51..127
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT   DOMAIN          135..196
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT   REGION          213..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..241
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   263 AA;  29124 MW;  6E5C30FAF6BAA9C2 CRC64;
     MDRKIVIPGQ LLSEKKEMAG PGTYVKNGNI YSLLYGIANF KGRVSVVPFS GKYIPSRKDF
     IIVNVIDVTP SNWIMETGSP YDGLLHVSEF PKRVDSSEMR KFMDVGDCVI VRVKDVSKAM
     KVELSMREQG SRALSKGRII EVVPSKVPRV IGHGGSMVSI LKKESNCDVF VGKNGRIWIN
     GKDKDMDRLT TAIEMIESES HMSGLTDKVG MFLRGEPEGT EGSDEEQLVD EEVAGVSLED
     DDVTEETSRK VDVLLDNDTD ETN