RRP41_PYRAB
ID RRP41_PYRAB Reviewed; 249 AA.
AC Q9V119; G8ZJ75;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=PYRAB06100;
GN ORFNames=PAB0420;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH RRP42, FUNCTION, AND
RP MUTAGENESIS OF ARG-89; LYS-91; ARG-137; ASP-186 AND ASP-204.
RX PubMed=18353775; DOI=10.1074/jbc.m801005200;
RA Navarro M.V., Oliveira C.C., Zanchin N.I., Guimaraes B.G.;
RT "Insights into the mechanism of progressive RNA degradation by the archaeal
RT exosome.";
RL J. Biol. Chem. 283:14120-14131(2008).
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:18353775}.
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; AJ248284; CAB49532.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70002.1; -; Genomic_DNA.
DR PIR; E75181; E75181.
DR RefSeq; WP_010867734.1; NC_000868.1.
DR PDB; 2PNZ; X-ray; 2.14 A; A=1-249.
DR PDB; 2PO0; X-ray; 2.30 A; A=1-249.
DR PDB; 2PO1; X-ray; 1.94 A; A=1-249.
DR PDB; 2PO2; X-ray; 2.41 A; A=1-249.
DR PDBsum; 2PNZ; -.
DR PDBsum; 2PO0; -.
DR PDBsum; 2PO1; -.
DR PDBsum; 2PO2; -.
DR AlphaFoldDB; Q9V119; -.
DR SMR; Q9V119; -.
DR STRING; 272844.PAB0420; -.
DR EnsemblBacteria; CAB49532; CAB49532; PAB0420.
DR GeneID; 1495515; -.
DR KEGG; pab:PAB0420; -.
DR PATRIC; fig|272844.11.peg.648; -.
DR eggNOG; arCOG01575; Archaea.
DR HOGENOM; CLU_063514_0_0_2; -.
DR OMA; KGKGQGW; -.
DR OrthoDB; 57069at2157; -.
DR PhylomeDB; Q9V119; -.
DR EvolutionaryTrace; Q9V119; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..249
FT /note="Exosome complex component Rrp41"
FT /id="PRO_0000139985"
FT MUTAGEN 89
FT /note="R->E: Does not affect ring assembly, but abolishes
FT RNA degradation; when associated with E-91."
FT /evidence="ECO:0000269|PubMed:18353775"
FT MUTAGEN 91
FT /note="K->E: Does not affect ring assembly, but abolishes
FT RNA degradation; when associated with E-89."
FT /evidence="ECO:0000269|PubMed:18353775"
FT MUTAGEN 137
FT /note="R->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:18353775"
FT MUTAGEN 186
FT /note="D->A: Abolishes RNA degradation."
FT /evidence="ECO:0000269|PubMed:18353775"
FT MUTAGEN 204
FT /note="D->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:18353775"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2PO0"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 50..61
FT /evidence="ECO:0007829|PDB:2PO1"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:2PO1"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2PO1"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:2PO1"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2PO1"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:2PO1"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2PO1"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:2PO1"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:2PO1"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:2PO1"
FT HELIX 209..241
FT /evidence="ECO:0007829|PDB:2PO1"
SQ SEQUENCE 249 AA; 27678 MW; ACB0748E1BF074A6 CRC64;
MMEKPEGLKL IDENGRRIDG RKKYELRPIK MEVGVLKNAN GSAYIEWGKN KIIAAVYGPR
ELHPKHLQRP DRAILRVRYN MAPFSVEERK KPGPDRRSIE ISKVIKGALE PALILEMFPR
TAIDVFIEVL QADAGTRVAG ITAASLALAD AGIPMRDLVA ACAAGKIEGE IVLDLNKEED
NYGEADVPVA IMPLKNDITL LQMDGYLTKD EFIEAVKLAI KGAKAVYQKQ REALKEKYLK
IAQEVEGSE
