ID   PELO_METM6              Reviewed;         348 AA.
AC   A9A8K6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=MmarC6_0862;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000867; ABX01679.1; -; Genomic_DNA.
DR   RefSeq; WP_012193634.1; NC_009975.1.
DR   AlphaFoldDB; A9A8K6; -.
DR   SMR; A9A8K6; -.
DR   STRING; 444158.MmarC6_0862; -.
DR   EnsemblBacteria; ABX01679; ABX01679; MmarC6_0862.
DR   GeneID; 5737928; -.
DR   KEGG; mmx:MmarC6_0862; -.
DR   eggNOG; arCOG01741; Archaea.
DR   HOGENOM; CLU_023334_0_0_2; -.
DR   OMA; DDLWHLK; -.
DR   OrthoDB; 90096at2157; -.
DR   PhylomeDB; A9A8K6; -.
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.
FT   CHAIN           1..348
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000361797"
SQ   SEQUENCE   348 AA;  39464 MW;  727AB4140798BDC3 CRC64;
     MKIIQEIPER NIIKLIPENL DDLWHLSNII QPYNAIYAVT ERRTEDKGDK LRADRGTKRR
     VFLGIKAEKI NFHEDFNRLR VSGKIIHAPD DIPIGSYHTI DIEPLLQVSV QKNWKKWDLA
     RLKDAEDSSK KPKVVVVIMD DSEADIFLVR EFGIKELASI KSGISKKLDY KQNEQAKFSY
     YSDIINSISE YEGKILFAGP GFGKNNIQNY ISEKHKDLAP NVVIESANHT GKSGLSEILK
     SGIIDKIYGE ARISKETQII EKLLEEISKK GLAAYGIESV SNAMNYSAID TLLLTDEYLR
     RNRRTIEELM NNVENINGNI LIISTEHDAG KQLKALGGIS ALLRFPIE