ID Q647V5_9ARCH Unreviewed; 228 AA.
AC Q647V5;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Exosome complex component Rrp4 {ECO:0000256|HAMAP-Rule:MF_00623};
GN Name=rrp4 {ECO:0000256|HAMAP-Rule:MF_00623};
GN ORFNames=GZ9D1_35 {ECO:0000313|EMBL:AAU84322.1};
OS uncultured archaeon GZfos9D1.
OC Archaea; environmental samples.
OX NCBI_TaxID=285356 {ECO:0000313|EMBL:AAU84322.1};
RN [1] {ECO:0000313|EMBL:AAU84322.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15353801; DOI=10.1126/science.1100025;
RA Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA Richardson P.M., DeLong E.F.;
RT "Reverse methanogenesis: testing the hypothesis with environmental
RT genomics.";
RL Science 305:1457-1462(2004).
RN [2] {ECO:0000313|EMBL:AAU84322.1}
RP NUCLEOTIDE SEQUENCE.
RA Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL Submitted (AUG-2004) 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; AY714871; AAU84322.1; -; Genomic_DNA.
DR AlphaFoldDB; Q647V5; -.
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 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; PF00013; KH_1; 1.
DR Pfam; PF21266; RRP4_S1; 1.
DR SMART; SM00322; KH; 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; PS50084; KH_TYPE_1; 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 RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00623}.
FT DOMAIN 57..130
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 228 AA; 25624 MW; 36C5B05C2F319206 CRC64;
MYQVVVPGDF LSEETKRAGE GTYVEEGKVY ASQYGIVSER GEIKVVSLSG KYMPSNGDVV
IGKITAISFP FWIVNLASPY EARLHVSALS GIAREKIEFG NMSEYLDVDD LVVVKVMDVN
VLMKIDLALQ EDLELRRGGR LIEIPHTKVP RVIGRSGSMI KMLKEKCNCF IFITKNGRIW
IRGKEDDMDL ASTVISKIAR ESHTSGLTDR VAEFLDSFRK EKERELRG
//
