ID   PELO_PYRCJ              Reviewed;         332 AA.
AC   A3MX13;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Pcal_1763;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000561; ABO09180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MX13; -.
DR   SMR; A3MX13; -.
DR   STRING; 410359.Pcal_1763; -.
DR   EnsemblBacteria; ABO09180; ABO09180; Pcal_1763.
DR   KEGG; pcl:Pcal_1763; -.
DR   eggNOG; arCOG01741; Archaea.
DR   HOGENOM; CLU_023334_0_0_2; -.
DR   OMA; DDLWHLK; -.
DR   Proteomes; UP000001431; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease.
FT   CHAIN           1..332
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000361815"
SQ   SEQUENCE   332 AA;  37752 MW;  5E0D1C4D53BC9826 CRC64;
     MKFELDEKRR VVRIVPEREE DLYFIYLLID RGDIVRGWTV REYKPEGAKE GERVKMYLGI
     SVEKIEYHKF RSSLRVRGTV VEVQEEVEGV KGRRHTFEIV PGREVVVEKR RGSVEVVKRI
     LDMANVALPR ILLVSIDDEE AALAYISALG AEIMYTVPNQ VNRGKRGESL LEDFFKSVNT
     LVEEVKRLRK IDRVVLAGPG MVVDQAGRYI RGERVVQSSG GVAGVYEFLR SGLYDKLKEE
     LGLEAYSRLQ KMLASQRDLV ALGVEEVKEA VSIGRAETVL ILDTYMKEKP DEAWEILSQV
     YNTGGKVYIV REDTEVGAAI RAMGNIVALL RW