ID A0A0T5ZGS5_9ARCH Unreviewed; 226 AA.
AC A0A0T5ZGS5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Exosome complex component Rrp4 {ECO:0000256|HAMAP-Rule:MF_00623};
GN Name=rrp4 {ECO:0000256|HAMAP-Rule:MF_00623};
GN ORFNames=XU09_C0001G0104 {ECO:0000313|EMBL:KRT62043.1};
OS Thaumarchaeota archaeon CSP1-1.
OC Archaea; Nitrososphaerota.
OX NCBI_TaxID=1640512 {ECO:0000313|EMBL:KRT62043.1, ECO:0000313|Proteomes:UP000051388};
RN [1] {ECO:0000313|EMBL:KRT62043.1, ECO:0000313|Proteomes:UP000051388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-1 {ECO:0000313|EMBL:KRT62043.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRT62043.1}.
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DR EMBL; LDXL01000001; KRT62043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZGS5; -.
DR STRING; 1640512.XU09_C0001G0104; -.
DR PATRIC; fig|1640512.3.peg.104; -.
DR Proteomes; UP000051388; Unassembled WGS sequence.
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; 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 PANTHER; PTHR21321:SF1; EXOSOME COMPLEX COMPONENT RRP40; 1.
DR PANTHER; PTHR21321; PNAS-3 RELATED; 1.
DR Pfam; PF00013; KH_1; 1.
DR SMART; SM00322; KH; 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; PS50084; KH_TYPE_1; 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 RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00623}.
FT DOMAIN 141..206
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
SQ SEQUENCE 226 AA; 24661 MW; 54E1A4807891EAEC CRC64;
MGDNKRRFVI PGEVITTGPY RPEQNVILEG KKIIATKVGI SEIYDDSVKV IPLTGKYIPK
SEDLVIGKII SHSSLSWEAD INSCYVGMLP GSDVFGRNFQ PDTDEMTSKL KKGDLIAARI
VNFDRSRDPL ITIADRELGK IDSGELVKIS PSKVPRLIGK QGTMIQAIEM ATHATITIGQ
NGLVVVACEN PDGLLKAKKA IQMIDEQAHM ANLTDKVKAM LESNSV
//
