ID   RRP41_METMA             Reviewed;         493 AA.
AC   Q8PTT8;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 116.
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=MM_2623;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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   -!- 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; AE008384; AAM32319.1; -; Genomic_DNA.
DR   RefSeq; WP_011034536.1; NC_003901.1.
DR   AlphaFoldDB; Q8PTT8; -.
DR   SMR; Q8PTT8; -.
DR   STRING; 192952.MM_2623; -.
DR   EnsemblBacteria; AAM32319; AAM32319; MM_2623.
DR   GeneID; 24879355; -.
DR   KEGG; mma:MM_2623; -.
DR   PATRIC; fig|192952.21.peg.3017; -.
DR   eggNOG; arCOG01575; Archaea.
DR   HOGENOM; CLU_541452_0_0_2; -.
DR   OMA; CYLEWGR; -.
DR   Proteomes; UP000000595; 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   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Exosome; Hydrolase; Nuclease; Reference proteome.
FT   CHAIN           1..493
FT                   /note="Exosome complex component Rrp41"
FT                   /id="PRO_0000139983"
FT   REGION          243..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..378
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..469
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  55249 MW;  979A757BEF8DC090 CRC64;
     MSNKPENLTL ITDDGLRLDG RRADEIRPMK IEVGVLSRAD GSCYLEWGRN KILVGVFGPR
     EAHPRRSQRA DSAVIRYRYN MASFSVEDRA RPGPSRRSIE ISKVSREAFE PVIMAELFPK
     TAIDIFVEVL QADAGTRTAA INASSIALAD AGIPMKGLIT SCAFGKVDGK IVLDLNKEED
     NYGEADFPVA MTQDGEITLI QMDGNLTPDE IKQGLELVKK GCKEILEIQQ AVLRKKFETP
     VEEVSEETAP EKGAEKEVLE PSPVAAIVEE TPEEAEEPEV EISEEVEAEI LASEVIPDFE
     DELEEEIEEE LEESEEDLET EEEEFEEEAL EEEAEPEEDL EEDLEEDLGE ELEEEEEELE
     EEEFEEEALE EETELEASLE CAPELKEFDE IEARLEKEDA SIEAEEEIEP EAEEATEEGL
     EEEAEIEETA ASEEENIEAE AEAEEEAEPE VEAEEISTEA EEAEEEPEEE KSEGPWKVVK
     DPSEAGTRGE KDE