RRP4_PYRAE
ID RRP4_PYRAE Reviewed; 235 AA.
AC Q8ZVM8;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Exosome complex component Rrp4 {ECO:0000255|HAMAP-Rule:MF_00623};
GN Name=rrp4 {ECO:0000255|HAMAP-Rule:MF_00623}; OrderedLocusNames=PAE2208;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(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; AE009441; AAL64028.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZVM8; -.
DR SMR; Q8ZVM8; -.
DR STRING; 178306.PAE2208; -.
DR EnsemblBacteria; AAL64028; AAL64028; PAE2208.
DR KEGG; pai:PAE2208; -.
DR PATRIC; fig|178306.9.peg.1640; -.
DR eggNOG; arCOG00678; Archaea.
DR HOGENOM; CLU_071769_0_0_2; -.
DR InParanoid; Q8ZVM8; -.
DR OMA; GPYIPEV; -.
DR Proteomes; UP000002439; 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; IPR026699; Exosome_RNA_bind1/RRP40/RRP4.
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; PF15985; KH_6; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exosome; Reference proteome; RNA-binding.
FT CHAIN 1..235
FT /note="Exosome complex component Rrp4"
FT /id="PRO_0000050151"
FT DOMAIN 63..137
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT DOMAIN 147..203
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
SQ SEQUENCE 235 AA; 26075 MW; CF751F97D8F05A52 CRC64;
MYYVTPRQLV FPGDVIATAD SKVEGPVYLD NGKYRSLVVG LVEFREDVVV VVPLEGTYKP
KKGDLVIGYV TDVLATGWEV DVRSFMPAYL PVGEALHRHV DLETTPLTTF LNIGDVVVAK
VKDVDLTDEY PIILTLKDEK VGKVESGTVV EITPVKVPRV IGKRGSMLNT LMELGCDIVV
GQNGRIWVKC KDPRDEVFLA SLIRKIEAES HVMGLTDRIR AEIENYKTSK QQGTV