ID D3TBQ8_ACIB4 Unreviewed; 270 AA.
AC D3TBQ8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Exosome complex component Rrp42 {ECO:0000256|HAMAP-Rule:MF_00622};
GN Name=rrp42 {ECO:0000256|HAMAP-Rule:MF_00622};
GN OrderedLocusNames=Aboo_0181 {ECO:0000313|EMBL:ADD07993.1};
OS Aciduliprofundum boonei (strain DSM 19572 / T469).
OC Archaea; Candidatus Thermoplasmatota; DHVE2 group; Aciduliprofundum.
OX NCBI_TaxID=439481 {ECO:0000313|EMBL:ADD07993.1, ECO:0000313|Proteomes:UP000001400};
RN [1] {ECO:0000313|Proteomes:UP000001400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19572 / T469 {ECO:0000313|Proteomes:UP000001400};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.;
RT "Complete sequence of Aciduliprofundum boonei T469.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-catalytic component of the exosome, which is a complex
CC involved in RNA degradation. Contributes to the structuring of the
CC Rrp41 active site. {ECO:0000256|HAMAP-Rule:MF_00622}.
CC -!- SUBUNIT: Component of the archaeal exosome complex. Forms a hexameric
CC ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers. The
CC hexameric ring associates with a trimer of Rrp4 and/or Csl4 subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00622}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00622}.
CC -!- SIMILARITY: Belongs to the RNase PH family. Rrp42 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00622}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001941; ADD07993.1; -; Genomic_DNA.
DR RefSeq; WP_012997062.1; NC_013926.1.
DR AlphaFoldDB; D3TBQ8; -.
DR GeneID; 8827119; -.
DR KEGG; abi:Aboo_0181; -.
DR HOGENOM; CLU_038194_0_0_2; -.
DR Proteomes; UP000001400; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd11365; RNase_PH_archRRP42; 1.
DR Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 1.
DR HAMAP; MF_00622; Exosome_Rrp42; 1.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR020869; Rrp42_archaea.
DR PANTHER; PTHR11097:SF8; EXOSOME COMPLEX COMPONENT RRP42; 1.
DR PANTHER; PTHR11097; EXOSOME COMPLEX EXONUCLEASE RIBOSOMAL RNA PROCESSING PROTEIN; 1.
DR Pfam; PF01138; RNase_PH; 1.
DR Pfam; PF03725; RNase_PH_C; 1.
DR SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00622};
KW Exosome {ECO:0000256|ARBA:ARBA00022835, ECO:0000256|HAMAP-Rule:MF_00622};
KW Reference proteome {ECO:0000313|Proteomes:UP000001400}.
FT DOMAIN 36..171
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF01138"
FT DOMAIN 187..251
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF03725"
SQ SEQUENCE 270 AA; 29316 MW; 2E91AEE2B0559291 CRC64;
MSNSKFTAGV VPEMQRKYIH KLASKGTRVD GRHFDEIRNL TVTKGYIPRA EGSALVNLGN
TRVLVGVKIE PGTPFPDTPN MGILTTNAEL APLASPTFEP GPPGEEAIEL ARVVDRGIRE
GHAIDLEKLV IEEGEKVWIV FIDIHVLDYD GNLFDAAGYG ALAALTNATV PASRYDLGED
FKLPVQHYPV PVTFAKIGDW IVADPNLDEE SIASARLTVA TNEEGKINAM QKGLSGTFTY
EEVKKVINMS MNIGGKVREI ILGDSNGKED
//