RRP4_PICTO
ID RRP4_PICTO Reviewed; 230 AA.
AC Q6L222;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Exosome complex component Rrp4 {ECO:0000255|HAMAP-Rule:MF_00623};
GN Name=rrp4 {ECO:0000255|HAMAP-Rule:MF_00623}; OrderedLocusNames=PTO0395;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT42980.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6L222; -.
DR SMR; Q6L222; -.
DR STRING; 263820.PTO0395; -.
DR EnsemblBacteria; AAT42980; AAT42980; PTO0395.
DR KEGG; pto:PTO0395; -.
DR PATRIC; fig|263820.9.peg.419; -.
DR eggNOG; arCOG00678; Archaea.
DR HOGENOM; CLU_071769_0_0_2; -.
DR OMA; GPYIPEV; -.
DR Proteomes; UP000000438; 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; 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 PANTHER; PTHR21321; PTHR21321; 1.
DR Pfam; PF00013; KH_1; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exosome; Reference proteome; RNA-binding.
FT CHAIN 1..230
FT /note="Exosome complex component Rrp4"
FT /id="PRO_0000416235"
FT DOMAIN 60..129
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT DOMAIN 137..195
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
SQ SEQUENCE 230 AA; 26139 MW; 560265648E64D5BB CRC64;
MEIRQIVYPG EKIDLEGQKP RNGLYEENDE YYSEYFGVVQ KSDKFIDIVP FNGPYMPRIN
DKVIGKVIDV SATMWTVDIN SPYFSLMHMN DTPWHVTSGD LRKYLNVGDY IYAKVSILNE
IKESWLSLKD VNLRKLEEGS IIYIKAPKVP RVIGKAGNMI NMIKSETNTK IIVGQNGLIW
IDGEPENVDL AINAIGMVEK EAHTFGLTDR VKAYLDKMKG GNNGRSEVNQ