ID A1RST1_PYRIL Unreviewed; 231 AA.
AC A1RST1;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Exosome complex component Rrp4 {ECO:0000256|HAMAP-Rule:MF_00623};
GN Name=rrp4 {ECO:0000256|HAMAP-Rule:MF_00623};
GN OrderedLocusNames=Pisl_0837 {ECO:0000313|EMBL:ABL88013.1};
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616 {ECO:0000313|EMBL:ABL88013.1, ECO:0000313|Proteomes:UP000002595};
RN [1] {ECO:0000313|Proteomes:UP000002595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3 {ECO:0000313|Proteomes:UP000002595};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|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 an hexameric
CC ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers.
CC {ECO:0000256|HAMAP-Rule:MF_00623}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00623}.
CC Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the RRP4 family. {ECO:0000256|ARBA:ARBA00009155,
CC ECO:0000256|HAMAP-Rule:MF_00623}.
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DR EMBL; CP000504; ABL88013.1; -; Genomic_DNA.
DR RefSeq; WP_011762589.1; NC_008701.1.
DR AlphaFoldDB; A1RST1; -.
DR STRING; 384616.Pisl_0837; -.
DR GeneID; 4616527; -.
DR KEGG; pis:Pisl_0837; -.
DR eggNOG; arCOG00678; Archaea.
DR HOGENOM; CLU_071769_0_0_2; -.
DR OrthoDB; 35160at2157; -.
DR Proteomes; UP000002595; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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; 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; 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; PF15985; KH_6; 1.
DR Pfam; PF21266; RRP4_S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF110324; Ribosomal L27 protein-like; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00623};
KW Exosome {ECO:0000256|ARBA:ARBA00022835, ECO:0000256|HAMAP-Rule:MF_00623};
KW Hydrolase {ECO:0000313|EMBL:ABL88013.1};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00623}.
FT DOMAIN 63..137
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 231 AA; 25737 MW; 2B21015DF6FE8AD5 CRC64;
MHLVVPRQLV FPGDVVATAE SRVEGPVYLD NGKYRSLVVG LVEFREDVVV IVPLEGTYRP
KKGDLVVGYV TDVLATGWEV DVRSFMPAYL PVSEALHKHV DLETTPLTTF LNIGDVIVAK
VKDVDLTDEY PIILTLKEEK VGKVERGTVI EISPVKVPRV IGKKGSMLNT LMELGCDIIV
GQNGRIWIRC RDVKDEVFLA SLVKKIEAES HVMGLTDRIK TEIEKWKTGK T
//
