ID   RRP4_METAC              Reviewed;         260 AA.
AC   Q8TPX7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Exosome complex component Rrp4 {ECO:0000255|HAMAP-Rule:MF_00623};
GN   Name=rrp4 {ECO:0000255|HAMAP-Rule:MF_00623}; OrderedLocusNames=MA_1777;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM05183.1; -; Genomic_DNA.
DR   RefSeq; WP_011021780.1; NC_003552.1.
DR   AlphaFoldDB; Q8TPX7; -.
DR   SMR; Q8TPX7; -.
DR   STRING; 188937.MA_1777; -.
DR   EnsemblBacteria; AAM05183; AAM05183; MA_1777.
DR   GeneID; 1473666; -.
DR   KEGG; mac:MA_1777; -.
DR   HOGENOM; CLU_071769_0_0_2; -.
DR   InParanoid; Q8TPX7; -.
DR   OMA; GPYIPEV; -.
DR   OrthoDB; 93052at2157; -.
DR   PhylomeDB; Q8TPX7; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR   GO; GO:0008143; F:poly(A) binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0071034; P:CUT catabolic process; IBA:GO_Central.
DR   GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
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   Pfam; PF00575; S1; 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..260
FT                   /note="Exosome complex component Rrp4"
FT                   /id="PRO_0000050146"
FT   DOMAIN          59..128
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT   DOMAIN          136..194
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
SQ   SEQUENCE   260 AA;  29136 MW;  84D40812F6A5221E CRC64;
     MDKKIVIPGD LLSENQKKAG YGTYVKNDKI YSSLCGIENL KEDKVGVIPL AGAYIPSAND
     VVIGIVIVVT PSNWIFDIAA PYDGLLHVSE YPRRVESREM PEILNVGDSV ILRVKDVDSS
     MKVELALRDP SLHKLKTGQI IKVESVKVPR VIGHGGSMIS MLKKETNCSI FVGQNGRIWI
     DGKDEDIELL SKALRKIELE AQRSGLTDRI YNFLKNERIR QKESKPVGFF KNETEGVTAT
     KEDHSEEIYR KIDVLLDPKN