ID   PELO_DESA1              Reviewed;         356 AA.
AC   B8D691;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=DKAM_1296;
OS   Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS   1221n) (Desulfurococcus kamchatkensis).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Desulfurococcus.
OX   NCBI_TaxID=490899;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n;
RX   PubMed=19114480; DOI=10.1128/jb.01525-08;
RA   Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA   Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Complete genome sequence of the anaerobic, protein-degrading
RT   hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL   J. Bacteriol. 191:2371-2379(2009).
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; CP001140; ACL11622.1; -; Genomic_DNA.
DR   RefSeq; WP_012608963.1; NC_011766.1.
DR   AlphaFoldDB; B8D691; -.
DR   SMR; B8D691; -.
DR   STRING; 490899.DKAM_1296; -.
DR   EnsemblBacteria; ACL11622; ACL11622; DKAM_1296.
DR   GeneID; 7171660; -.
DR   KEGG; dka:DKAM_1296; -.
DR   eggNOG; arCOG01741; Archaea.
DR   HOGENOM; CLU_023334_0_0_2; -.
DR   OMA; DDLWHLK; -.
DR   Proteomes; UP000006903; 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..356
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_1000188677"
SQ   SEQUENCE   356 AA;  39905 MW;  C547AD6A5D9B731A CRC64;
     MRVLEEDLRN GYIRILVEDI DDLWILFMVL RKGDIVYART SREVKPGEGG SSRRIPMVLG
     LRVEAIEFQE FTEKLRIRGI VVEGPEEFGV KGHYHTIAIG VGDQLAIVRE TWSKHSLDIL
     KKGVRRRRIL LVSIDYDSAC IAVLTEQGVK HHSEIQSDLP GKMYRVEHEE ILDEYLSKVA
     SALNNVIQQE EIDAVIIAGP GDLKNKLGEN IRRDNRKHVY LDTTSTGGCQ GISELLGRDV
     VKQVVGDLSI VKAKEVVEEF KRLIIKDPQL VAYGVDDVYG AVVYAAVSRI VVAGDLLHEP
     DDERRARVYE ILEKAYETGA EVIIVPGKSD VGLEVQGFGG VIAVLRYRLF RGEHSP