PELO_PICTO
ID PELO_PICTO Reviewed; 339 AA.
AC Q6L2M8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, 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=PTO0189;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT42774.1; -; Genomic_DNA.
DR RefSeq; WP_011176990.1; NC_005877.1.
DR AlphaFoldDB; Q6L2M8; -.
DR SMR; Q6L2M8; -.
DR STRING; 263820.PTO0189; -.
DR EnsemblBacteria; AAT42774; AAT42774; PTO0189.
DR GeneID; 2844490; -.
DR KEGG; pto:PTO0189; -.
DR eggNOG; arCOG01741; Archaea.
DR HOGENOM; CLU_023334_0_0_2; -.
DR OMA; DDLWHLK; -.
DR OrthoDB; 90096at2157; -.
DR Proteomes; UP000000438; 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;
KW Reference proteome.
FT CHAIN 1..339
FT /note="Protein pelota homolog"
FT /id="PRO_0000361812"
SQ SEQUENCE 339 AA; 39325 MW; 659B84A6689CB3FD CRC64;
MKINIDEKLE TTEILIETQD DLWYIKNILN PGDIIEGIAY RRLEKRNDLE RSKSTERIPI
KVKIKIENLD FQPFTDKIKI LGIIIDGDFS GEHQSIMYGP GDTLKIYKNL NEAERDFLNE
AVKNEYSSGM IFVSLDEEAA DIYLMRSYSL QDMAHIESNK TGKRYDLKYN EKQYFLDIIK
ALKNIKNVFL LIVLGTGFEP EKLYNEIKKD PFFNNIDVKF YNTYDTGKSG VYNLLNSDAT
SNIIKESRMA KEKRILETFL RNLNSGLSVY GYDEINNYLD NGAIDTLIIS EEKFKMPETR
ELLNKASGIK IYIISNYTEP GEIIRSFGGY CAILRYKIK