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Database: UniProt
Entry: I0A2W9_FERFK
LinkDB: I0A2W9_FERFK
Original site: I0A2W9_FERFK 
ID   I0A2W9_FERFK            Unreviewed;       246 AA.
AC   I0A2W9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Exosome complex component Rrp41 {ECO:0000256|HAMAP-Rule:MF_00591};
DE            EC=3.1.13.- {ECO:0000256|HAMAP-Rule:MF_00591};
GN   Name=rrp41 {ECO:0000256|HAMAP-Rule:MF_00591};
GN   OrderedLocusNames=FFONT_1338 {ECO:0000313|EMBL:AFH43326.1};
OS   Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / Kam940).
OC   Archaea; Thermoproteota; Thermoprotei; Fervidicoccales; Fervidicoccaceae;
OC   Fervidicoccus.
OX   NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH43326.1, ECO:0000313|Proteomes:UP000007391};
RN   [1] {ECO:0000313|Proteomes:UP000007391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC   {ECO:0000313|Proteomes:UP000007391};
RA   Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., Kublanov I.V.,
RA   Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Fervidicoccus fontis complete genome analysis confirms its distinct
RT   phylogenetic position and predicts its environmental function.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFH43326.1, ECO:0000313|Proteomes:UP000007391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC   {ECO:0000313|Proteomes:UP000007391};
RX   PubMed=24366681; DOI=10.1007/s00792-013-0616-7;
RA   Lebedinsky A.V., Mardanov A.V., Kublanov I.V., Gumerov V.M., Beletsky A.V.,
RA   Perevalova A.A., Bidzhieva S.Kh., Bonch-Osmolovskaya E.A., Skryabin K.G.,
RA   Ravin N.V.;
RT   "Analysis of the complete genome of Fervidococcus fontis confirms the
RT   distinct phylogenetic position of the order Fervidicoccales and suggests
RT   its environmental function.";
RL   Extremophiles 18:295-309(2014).
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 heteropolymeric RNA-tails. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00591}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00591}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. Rrp41 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00591}.
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DR   EMBL; CP003423; AFH43326.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0A2W9; -.
DR   STRING; 1163730.FFONT_1338; -.
DR   KEGG; ffo:FFONT_1338; -.
DR   eggNOG; arCOG01575; Archaea.
DR   HOGENOM; CLU_063514_0_0_2; -.
DR   InParanoid; I0A2W9; -.
DR   OrthoDB; 24266at2157; -.
DR   Proteomes; UP000007391; 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'-RNA exonuclease 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; GHMP Kinase, N-terminal domain; 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_Su5_D2-typ_SF.
DR   InterPro; IPR011807; Rrp41.
DR   NCBIfam; TIGR02065; ECX1; 1.
DR   PANTHER; PTHR11953; EXOSOME COMPLEX COMPONENT; 1.
DR   PANTHER; PTHR11953:SF2; EXOSOME COMPLEX COMPONENT MTR3; 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|HAMAP-Rule:MF_00591};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_00591};
KW   Exosome {ECO:0000256|ARBA:ARBA00022835, ECO:0000256|HAMAP-Rule:MF_00591};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00591};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007391}.
FT   DOMAIN          24..153
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF01138"
FT   DOMAIN          156..221
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF03725"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   246 AA;  27173 MW;  47A9D7D005A59426 CRC64;
     MSHNSNRKLI DENGLRVDGR RPDQLRPISM KVGILKNAQG SALVSYGKTQ VMAAVYGPRE
     ALPRHMTLPD RAILRIRYHM APFSTSERKS PAPTRREIEL SKVIREALEA TVFSELFPRT
     TIDVFIEVLQ ADGGTRTTSL TAASLALADA GIPMKDLIAG VAVGKVDGVL VLDINEIEDS
     TGQADMPVAI MPNLNKIVLL QLNGTLTRDE FNEALKMAQK AIKEIYIMQK EALREKYSSM
     EEVEQA
//
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