ID   PELO_HALWD              Reviewed;         355 AA.
AC   Q18J81;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=HQ_1802A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(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; AM180088; CAJ51930.1; -; Genomic_DNA.
DR   RefSeq; WP_011571077.1; NC_008212.1.
DR   AlphaFoldDB; Q18J81; -.
DR   SMR; Q18J81; -.
DR   STRING; 362976.HQ_1802A; -.
DR   EnsemblBacteria; CAJ51930; CAJ51930; HQ_1802A.
DR   GeneID; 4194414; -.
DR   KEGG; hwa:HQ_1802A; -.
DR   eggNOG; arCOG01741; Archaea.
DR   HOGENOM; CLU_023334_0_0_2; -.
DR   OMA; DDLWHLK; -.
DR   Proteomes; UP000001975; 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..355
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000361786"
SQ   SEQUENCE   355 AA;  39258 MW;  8E65A6BC868A2EB0 CRC64;
     MRIPSRGRGE EGKEQWTLVP ENVDDLWHLS HVLEPGDRVG GDTTRRIQRN DENLRDTGGQ
     REHLVVTIEV ADVEFARFAN RLRVGGEIIS CSREDELGHY HTLNVESHDE IIVTKKFAPD
     QRKRIEAAEE AAENADVAVA TIEEGEAHIH TVAQYGTEEQ FSRTATTGKG EYSQPRTELF
     AEFAAALSRM DVDAIILAGP GFTKQDAEEY IQSNNPEIID KLTIVDTAAV GDRGVHEVLK
     RGAVDEVQTQ TRISAEAELI DELMEGIATG EKIAYGIDEV AKAAEFGAVD DLLVVDDQLR
     EERRDSGDWS TDVDTVLQNV EQQGGSVTVL SGEFDPGQRL RNLGGIAALL RYRLQ