RRP41_METTH
ID RRP41_METTH Reviewed; 240 AA.
AC O26779;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=MTH_683;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH RRP42.
RX PubMed=20445227; DOI=10.1107/s0907444910002908;
RA Ng C.L., Waterman D.G., Antson A.A., Ortiz-Lombardia M.;
RT "Structure of the Methanothermobacter thermautotrophicus exosome RNase PH
RT ring.";
RL Acta Crystallogr. D 66:522-528(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. {ECO:0000255|HAMAP-
CC Rule:MF_00591}.
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}.
CC -!- INTERACTION:
CC O26779; O26778: rrp42; NbExp=2; IntAct=EBI-764220, EBI-764215;
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}.
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; AE000666; AAB85188.1; -; Genomic_DNA.
DR PIR; A69191; A69191.
DR RefSeq; WP_010876322.1; NC_000916.1.
DR PDB; 2WNR; X-ray; 2.65 A; B/D/F=1-240.
DR PDBsum; 2WNR; -.
DR AlphaFoldDB; O26779; -.
DR SMR; O26779; -.
DR DIP; DIP-33665N; -.
DR IntAct; O26779; 2.
DR STRING; 187420.MTH_683; -.
DR PRIDE; O26779; -.
DR EnsemblBacteria; AAB85188; AAB85188; MTH_683.
DR GeneID; 24853825; -.
DR KEGG; mth:MTH_683; -.
DR PATRIC; fig|187420.15.peg.664; -.
DR HOGENOM; CLU_063514_0_0_2; -.
DR OMA; KGKGQGW; -.
DR EvolutionaryTrace; O26779; -.
DR Proteomes; UP000005223; 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..240
FT /note="Exosome complex component Rrp41"
FT /id="PRO_0000139984"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 50..61
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2WNR"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:2WNR"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2WNR"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:2WNR"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 160..174
FT /evidence="ECO:0007829|PDB:2WNR"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:2WNR"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:2WNR"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:2WNR"
FT HELIX 209..235
FT /evidence="ECO:0007829|PDB:2WNR"
SQ SEQUENCE 240 AA; 26524 MW; 2D59F8ABD2BD5DF7 CRC64;
MITIITQDQL KTSPSVREDG RAFDELRPLK IEAGILERAD GSSYLEFGGN KILVAVYGPR
EAQIRKLQRP DRAVIRCRYN MAPFSVEERK RPGPDRRSVE ISKITAEALR PALILEKFPR
SVIDVFIEVL EAEGGTRCAG ITAASVALAD AGIPMRDMVV ACAAGKVGDQ VVLDLSEEED
KEGQADVPVA ILPRTREITL LQSDGNLTPE EFERALDLAV EGCLRIHEVQ KEALRKRYGE
