PELO_METAR
ID PELO_METAR Reviewed; 357 AA.
AC Q0W6H4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Protein pelota homolog {ECO:0000255|HAMAP-Rule:MF_01853};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01853};
GN Name=pelA {ECO:0000255|HAMAP-Rule:MF_01853}; OrderedLocusNames=UNCMA_21660;
GN ORFNames=RCIX613;
OS Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=351160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX PubMed=16857943; DOI=10.1126/science.1127062;
RA Erkel C., Kube M., Reinhardt R., Liesack W.;
RT "Genome of rice cluster I archaea -- the key methane producers in the rice
RT rhizosphere.";
RL Science 313:370-372(2006).
CC -!- FUNCTION: May function in recognizing stalled ribosomes, interact with
CC stem-loop structures in stalled mRNA molecules, and effect
CC endonucleolytic cleavage of the mRNA. May play a role in the release
CC non-functional ribosomes and degradation of damaged mRNAs. Has
CC endoribonuclease activity. {ECO:0000255|HAMAP-Rule:MF_01853}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01853};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01853}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01853}.
CC -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC the endoribonuclease activity. {ECO:0000255|HAMAP-Rule:MF_01853}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01853}.
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DR EMBL; AM114193; CAJ36019.1; -; Genomic_DNA.
DR RefSeq; WP_012036488.1; NC_009464.1.
DR AlphaFoldDB; Q0W6H4; -.
DR SMR; Q0W6H4; -.
DR STRING; 351160.RCIX613; -.
DR PRIDE; Q0W6H4; -.
DR EnsemblBacteria; CAJ36019; CAJ36019; RCIX613.
DR GeneID; 5144046; -.
DR KEGG; rci:RCIX613; -.
DR PATRIC; fig|351160.9.peg.2217; -.
DR eggNOG; arCOG01741; Archaea.
DR OMA; DDLWHLK; -.
DR OrthoDB; 90096at2157; -.
DR Proteomes; UP000000663; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IEA:InterPro.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:InterPro.
DR GO; GO:0071025; P:RNA surveillance; IEA:InterPro.
DR Gene3D; 2.30.30.870; -; 1.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.420.60; -; 1.
DR HAMAP; MF_01853; PelO; 1.
DR InterPro; IPR042226; eFR1_2_sf.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR038069; Pelota/DOM34_N.
DR InterPro; IPR023521; Pelota_arc.
DR InterPro; IPR004405; Transl-rel_pelota.
DR PANTHER; PTHR10853; PTHR10853; 1.
DR Pfam; PF03463; eRF1_1; 1.
DR Pfam; PF03464; eRF1_2; 1.
DR Pfam; PF03465; eRF1_3; 1.
DR SMART; SM01194; eRF1_1; 1.
DR SUPFAM; SSF159065; SSF159065; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR TIGRFAMs; TIGR00111; pelota; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..357
FT /note="Protein pelota homolog"
FT /id="PRO_0000361828"
SQ SEQUENCE 357 AA; 39844 MW; C9B300E6E4E42F24 CRC64;
MKVNKEEYRG DYGEISLQPE SLDDLWHLKY IVEPGDTVFA MTFRAVDSVS DKIRPDKVEK
KLVRLGIKVE STEFHKFSNR LRIKGTIISD LDAGAYHTLN IEPYSELSIA KHWKSDQIER
IRDAVEASKR PEVEIVTIEE GEAAIGYLRQ YGIEEVSRIR QASSGKREGA DARSVDGRGE
FFGEVAAQLK YADKVQTIVV AGPGFIKDDF VKFLRVNHPA VAQKVIVEDT SSIGSSGFQE
VLRRGAIQRV AEENRITREA QLIEALLSEI AKDGKATYGF AETKRAVDYG AVETLLIADE
TLRGLREKGA RDIESLMRDV EHARGKVVVF STEFEPGQRL EKLGGVASIL RFPIGGD