RRP41_ARCFU
ID RRP41_ARCFU Reviewed; 258 AA.
AC O29757;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Exosome complex component Rrp41 {ECO:0000255|HAMAP-Rule:MF_00591};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_00591};
GN Name=rrp41 {ECO:0000255|HAMAP-Rule:MF_00591}; OrderedLocusNames=AF_0493;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH RRP42; RRP4 AND
RP CSL4, FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-65 AND ASP-180.
RX PubMed=16285927; DOI=10.1016/j.molcel.2005.10.018;
RA Buttner K., Wenig K., Hopfner K.P.;
RT "Structural framework for the mechanism of archaeal exosomes in RNA
RT processing.";
RL Mol. Cell 20:461-471(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH RRP42 AND CSL4, AND
RP SUBUNIT.
RX PubMed=20392821; DOI=10.1093/nar/gkq238;
RA Hartung S., Niederberger T., Hartung M., Tresch A., Hopfner K.P.;
RT "Quantitative analysis of processive RNA degradation by the archaeal RNA
RT exosome.";
RL Nucleic Acids Res. 38:5166-5176(2010).
CC -!- FUNCTION: Catalytic component of the exosome, which is a complex
CC involved in RNA degradation. Has 3'->5' exoribonuclease activity. Can
CC also synthesize heteromeric RNA-tails (Probable).
CC {ECO:0000305|PubMed:16285927}.
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:0000255|HAMAP-Rule:MF_00591, ECO:0000269|PubMed:16285927,
CC ECO:0000269|PubMed:20392821}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00591}.
CC -!- SIMILARITY: Belongs to the RNase PH family. Rrp41 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00591}.
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DR EMBL; AE000782; AAB90744.1; -; Genomic_DNA.
DR PIR; E69311; E69311.
DR RefSeq; WP_010878000.1; NC_000917.1.
DR PDB; 2BA0; X-ray; 2.70 A; D/E/F=1-258.
DR PDB; 2BA1; X-ray; 2.70 A; D/E/F=1-258.
DR PDB; 3M7N; X-ray; 2.40 A; D/E/F=1-258.
DR PDB; 3M85; X-ray; 3.00 A; D/E/F=1-258.
DR PDBsum; 2BA0; -.
DR PDBsum; 2BA1; -.
DR PDBsum; 3M7N; -.
DR PDBsum; 3M85; -.
DR AlphaFoldDB; O29757; -.
DR SMR; O29757; -.
DR STRING; 224325.AF_0493; -.
DR PRIDE; O29757; -.
DR EnsemblBacteria; AAB90744; AAB90744; AF_0493.
DR GeneID; 24794033; -.
DR KEGG; afu:AF_0493; -.
DR eggNOG; arCOG01575; Archaea.
DR HOGENOM; CLU_063514_0_0_2; -.
DR OMA; KGKGQGW; -.
DR OrthoDB; 57069at2157; -.
DR PhylomeDB; O29757; -.
DR EvolutionaryTrace; O29757; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd11366; RNase_PH_archRRP41; 1.
DR Gene3D; 3.30.230.70; -; 1.
DR HAMAP; MF_00591; Exosome_Rrp41; 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_S5_D2-typ_fold.
DR InterPro; IPR011807; Rrp41.
DR Pfam; PF01138; RNase_PH; 1.
DR Pfam; PF03725; RNase_PH_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55666; SSF55666; 1.
DR TIGRFAMs; TIGR02065; ECX1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Exonuclease; Exosome; Hydrolase; Nuclease;
KW Reference proteome.
FT CHAIN 1..258
FT /note="Exosome complex component Rrp41"
FT /id="PRO_0000139981"
FT MUTAGEN 65
FT /note="R->E: Reduces RNA degradation more than 90%.
FT Abolishes RNA binding by the Rrp41-Rrp42 ring."
FT /evidence="ECO:0000269|PubMed:16285927"
FT MUTAGEN 180
FT /note="D->A: Abolishes exoribonuclease activity."
FT /evidence="ECO:0000269|PubMed:16285927"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 50..61
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:3M7N"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3M7N"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:3M7N"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:3M7N"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 155..167
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:3M7N"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 183..194
FT /evidence="ECO:0007829|PDB:3M7N"
FT STRAND 197..210
FT /evidence="ECO:0007829|PDB:3M7N"
FT HELIX 212..249
FT /evidence="ECO:0007829|PDB:3M7N"
SQ SEQUENCE 258 AA; 28847 MW; 592BD6A3DB2128B3 CRC64;
MSEFNEKPEK LIVDGLRLDG RKFDELRPIK IEASVLKRAD GSCYLEMGKN KVIAAVFGPR
EVHPRHLQDP SKAIIRYRYN MAPFSVEERK RPGPDRRSIE ISKVSKEAFE AVIMKELFPR
SAIDIFVEVL QADAGSRTAC LNAASVALVD AGVPMKGMIT SVAVGKADGQ LVLDPMKEED
NFGEADMPFA FLIRNGKIES IALLQMDGRM TRDEVKQAIE LAKKGALQIY EMQREAILRR
YIEVGEEMDE ITEGGEDA
