RRP4_PYRHO
ID RRP4_PYRHO Reviewed; 265 AA.
AC O59221;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Exosome complex component Rrp4 {ECO:0000255|HAMAP-Rule:MF_00623};
GN Name=rrp4 {ECO:0000255|HAMAP-Rule:MF_00623}; OrderedLocusNames=PH1551;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30663.1; -; Genomic_DNA.
DR PIR; G71032; G71032.
DR RefSeq; WP_010885630.1; NC_000961.1.
DR AlphaFoldDB; O59221; -.
DR SMR; O59221; -.
DR STRING; 70601.3257980; -.
DR EnsemblBacteria; BAA30663; BAA30663; BAA30663.
DR GeneID; 1443870; -.
DR KEGG; pho:PH1551; -.
DR eggNOG; arCOG00678; Archaea.
DR OMA; GPYIPEV; -.
DR OrthoDB; 93052at2157; -.
DR Proteomes; UP000000752; 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 InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR21321; PTHR21321; 1.
DR Pfam; PF15985; KH_6; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exosome; RNA-binding.
FT CHAIN 1..265
FT /note="Exosome complex component Rrp4"
FT /id="PRO_0000050153"
FT DOMAIN 65..137
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT DOMAIN 147..205
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 265 AA; 29649 MW; E4C46D4C8849D401 CRC64;
MKRIFVQNRE LVVPGTLLAQ GPYKNGRGTF REGSRIYSTV IGLVDIKGNT IRVIPLEGPY
IPEVGDNVIG KIVDVKFSSW VVDIGAPYLA NLKIQDFTDE KIDLLRTDLR KFFDIGDIIY
GKVKAITEVN NIDLTTKGMP FNGGPLKGGQ IVKITPSRVP RVIGRGGSMI NMIKKLTMTR
IIVGQNGWIW VNGKNEALEK LAIEAILKID RESHTKGLTD RIKSLLLSRL QELKEKGVIE
EIPELEEEPQ EETEVNNNDG ETRRT