ID RRP4_PYRFU Reviewed; 264 AA.
AC Q8U0L8;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Exosome complex component Rrp4 {ECO:0000255|HAMAP-Rule:MF_00623};
GN Name=rrp4 {ECO:0000255|HAMAP-Rule:MF_00623}; OrderedLocusNames=PF1569;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL81693.1; -; Genomic_DNA.
DR RefSeq; WP_011012715.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U0L8; -.
DR SMR; Q8U0L8; -.
DR STRING; 186497.PF1569; -.
DR PaxDb; 186497-PF1569; -.
DR GeneID; 41713393; -.
DR KEGG; pfu:PF1569; -.
DR PATRIC; fig|186497.12.peg.1635; -.
DR eggNOG; arCOG00678; Archaea.
DR HOGENOM; CLU_071769_0_0_2; -.
DR OrthoDB; 35160at2157; -.
DR PhylomeDB; Q8U0L8; -.
DR Proteomes; UP000001013; 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 CDD; cd22524; KH-I_Rrp4_prokar; 1.
DR CDD; cd05789; S1_Rrp4; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR048565; RRP4_S1.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR21321:SF1; EXOSOME COMPLEX COMPONENT RRP40; 1.
DR PANTHER; PTHR21321; PNAS-3 RELATED; 1.
DR Pfam; PF14382; ECR1_N; 1.
DR Pfam; PF15985; KH_6; 1.
DR Pfam; PF21266; RRP4_S1; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF110324; Ribosomal L27 protein-like; 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..264
FT /note="Exosome complex component Rrp4"
FT /id="PRO_0000050152"
FT DOMAIN 65..137
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT DOMAIN 147..206
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT REGION 244..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 264 AA; 29534 MW; 78492470BE197C70 CRC64;
MRRIFVQNRE LVVPGTLLAQ GPYKNGRGTF KEGSRIYSTV IGLVDIKGNT IRVIPLEGPY
IPEVGDNVLG KIVDVKFSSW TVDIGSPYSA TLKIQDYTDE KIDLLRTDLR KFFDIGDIIY
AKVKGINEVN NIELTTKGMP FNGGPLRGGQ IIKITSSKVP RVIGKGGSMI NMIKKLTQSR
IIVGQNGWIW ISSKNPELEK LAIEAILKIE RESHTRGLTD RIKNMLLSKL QELKERGVIE
EIPSLEEETQ EETVMENDVE ARGP
//
