ID   PELO_THEKO              Reviewed;         357 AA.
AC   Q5JIB9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=TK0964;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD85153.1; -; Genomic_DNA.
DR   RefSeq; WP_011249915.1; NC_006624.1.
DR   PDB; 3J15; EM; 6.60 A; A=2-357.
DR   PDBsum; 3J15; -.
DR   AlphaFoldDB; Q5JIB9; -.
DR   SMR; Q5JIB9; -.
DR   STRING; 69014.TK0964; -.
DR   EnsemblBacteria; BAD85153; BAD85153; TK0964.
DR   GeneID; 3233770; -.
DR   KEGG; tko:TK0964; -.
DR   PATRIC; fig|69014.16.peg.942; -.
DR   eggNOG; arCOG01741; Archaea.
DR   HOGENOM; CLU_023334_0_0_2; -.
DR   InParanoid; Q5JIB9; -.
DR   OMA; DDLWHLK; -.
DR   OrthoDB; 90096at2157; -.
DR   PhylomeDB; Q5JIB9; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070651; P:nonfunctional rRNA decay; IBA:GO_Central.
DR   GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IBA:GO_Central.
DR   GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:InterPro.
DR   GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..357
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000361820"
SQ   SEQUENCE   357 AA;  40605 MW;  64ADA448D7F4C6BD CRC64;
     MQILEEKPKE GKVKVKAETL DDLWHLYHII DPGDIVYAKT LRKQAQRADS LRAEKVEVIP
     VFLGVQAEKI NFHKFANQVR VTGPIVYASR EDVPLGKYHT IAIEQGTVVT IQKPRWKEHH
     IERLKEAVAA SKRARVMIVV IDDGEADMAL VREYGVEILN SIRHNLGGKR YNTDRESEEM
     KFFHDVAKTM EEVMKRENVE KAIVAGPGFV KEDFYKFLKE KYPELAKKVV IEDTSVTGRT
     GIYEVIKRGV VDRVYQENRV AKEVQLVEKV LENIARNNGL VAYGLKEVEE AVNYGAVETL
     LVLDELLKGE LREKVEELMD AVRYSRGEVV VVSSEHEGGE KLKALGGLAA LLRFRVK