ID A3DMV0_STAMF Unreviewed; 285 AA.
AC A3DMV0;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Exosome complex component Rrp42 {ECO:0000256|HAMAP-Rule:MF_00622};
GN Name=rrp42 {ECO:0000256|HAMAP-Rule:MF_00622};
GN OrderedLocusNames=Smar_0860 {ECO:0000313|EMBL:ABN69960.1};
OS Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=399550 {ECO:0000313|EMBL:ABN69960.1, ECO:0000313|Proteomes:UP000000254};
RN [1] {ECO:0000313|Proteomes:UP000000254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1
RC {ECO:0000313|Proteomes:UP000000254};
RX PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA Woese C., Bristow J., Kyrpides N.;
RT "The complete genome sequence of Staphylothermus marinus reveals
RT differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL BMC Genomics 10:145-145(2009).
RN [2] {ECO:0000313|EMBL:ABN69960.1, ECO:0000313|Proteomes:UP000000254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1
RC {ECO:0000313|Proteomes:UP000000254};
RX PubMed=21304655; DOI=10.4056/sigs.30527;
RA Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT type strain F1.";
RL Stand. Genomic Sci. 1:183-188(2009).
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}.
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DR EMBL; CP000575; ABN69960.1; -; Genomic_DNA.
DR RefSeq; WP_011839151.1; NC_009033.1.
DR AlphaFoldDB; A3DMV0; -.
DR STRING; 399550.Smar_0860; -.
DR GeneID; 4907882; -.
DR KEGG; smr:Smar_0860; -.
DR eggNOG; arCOG01574; Archaea.
DR HOGENOM; CLU_038194_0_0_2; -.
DR OrthoDB; 30932at2157; -.
DR Proteomes; UP000000254; 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: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 Hydrolase {ECO:0000313|EMBL:ABN69960.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000254}.
FT DOMAIN 36..171
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF01138"
FT DOMAIN 198..261
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF03725"
SQ SEQUENCE 285 AA; 31801 MW; A0B0C86486D6714D CRC64;
MSLTPTRQPI VPKIKHETIK KLLKQGERID GRKLDEYRPI EVFLNPIPKA EGSAAVKLGN
TFVITGVKLE IGTPYSDRPN EGVLQVHAEF VPLASPTFEP GPPDENAIET ARVIDRSLRE
PRAIRLEDLV VIPGKKVWLI FNDLYLIDHY GNIVDTGMLS TMLALNMTKI PRIVSIEDEN
VVIDKTVKEA PLPLNLNVVT VTLGIIDDVI IVDPNIEEEL VVDSRITFAV DETNRIVGIQ
KMGMKGIKPK MIDQLVDIAL KKASELHSLL REVLNNPDTY IKTLV
//