PELO_PYRAE
ID PELO_PYRAE Reviewed; 332 AA.
AC Q8ZTE8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=PAE3287;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64813.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZTE8; -.
DR SMR; Q8ZTE8; -.
DR STRING; 178306.PAE3287; -.
DR EnsemblBacteria; AAL64813; AAL64813; PAE3287.
DR KEGG; pai:PAE3287; -.
DR PATRIC; fig|178306.9.peg.2475; -.
DR eggNOG; arCOG01741; Archaea.
DR HOGENOM; CLU_023334_0_0_2; -.
DR InParanoid; Q8ZTE8; -.
DR OMA; DDLWHLK; -.
DR Proteomes; UP000002439; 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; 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..332
FT /note="Protein pelota homolog"
FT /id="PRO_0000361813"
SQ SEQUENCE 332 AA; 37811 MW; A125C4D01BF598C4 CRC64;
MKYEIDKKRL VIRVVPEREE DLYFIYLLID KGDIIRGWTV REYKPDGVKE GERIKMYLAI
KAEALEYHKF RGSLRVRGPV IEVQEGVEGV KGRRHTFDIS IGREIEIEKN EDKPLEVVDE
ILNMAKNVMP RILLISIDDE EAAFAYITSI GVNVLHVVRN DAERSRGDSL LHDYLVTIGK
IAEDLKRRLN PDKVVVTGPH IVVEQIGNYV RGDRVAQSVG GLAGIYEFMR AGLYDGLKTE
MGIKAYERLM QLLATERNLV AIGLEEVEMA VAAGRVEILL IVDSYIKEDP HRAWDLIYKV
YATRGKIYII REDLEIGTSL KAMGGVASIL RW