ID   PELO_METS5              Reviewed;         341 AA.
AC   A4YIP3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Msed_2156;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP96295.1; -; Genomic_DNA.
DR   RefSeq; WP_012022082.1; NC_009440.1.
DR   AlphaFoldDB; A4YIP3; -.
DR   SMR; A4YIP3; -.
DR   STRING; 399549.Msed_2156; -.
DR   EnsemblBacteria; ABP96295; ABP96295; Msed_2156.
DR   GeneID; 5104895; -.
DR   GeneID; 59456704; -.
DR   KEGG; mse:Msed_2156; -.
DR   eggNOG; arCOG01741; Archaea.
DR   HOGENOM; CLU_023334_0_0_2; -.
DR   OMA; DDLWHLK; -.
DR   Proteomes; UP000000242; 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; 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; 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..341
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000361790"
SQ   SEQUENCE   341 AA;  38575 MW;  CE65D056A22F1340 CRC64;
     MKILEYDEKT GALRLHVENE DDLWLIHLVL SKGDIVVART TRDVSMGNDS RRVPMVVELE
     VEFSEFQPFT SRLRIHGIVR DAPERYGIKG SHHTINLDIG DEIVIIKKWT KGLIDRIRKQ
     AEKNKRVLIV LTDQDELLVA LPMEQGIRIL TERSLPGVSD EDKSLESVAL EVSKEVEQYV
     KQYSPDAVII AGPGPFKEIV RDKLKIKPRI YVDNVSSASR AGLNEILRRD IIDEVMRDYQ
     ISVASRELER GLSLLAQGSS LVVYGRDEVE RASQIGAVET LLVTDDLLTL EDEETRRKTE
     AIMEAVESKG GKVMIVPKDS PVYLQLKNLT GLLAILRFRI N