ID   PELO_CAEEL              Reviewed;         381 AA.
AC   P50444;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Protein pelota homolog {ECO:0000250|UniProtKB:P48612};
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN   Name=pelo-1 {ECO:0000312|WormBase:R74.6};
GN   ORFNames=R74.6 {ECO:0000312|WormBase:R74.6};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Required for normal chromosome segregation during cell
CC       division and genomic stability. May function in recognizing stalled
CC       ribosomes and triggering endonucleolytic cleavage of the mRNA, a
CC       mechanism to release non-functional ribosomes and degrade damaged
CC       mRNAs. May have ribonuclease activity. {ECO:0000250|UniProtKB:P33309,
CC       ECO:0000250|UniProtKB:Q80X73}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P33309};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P48612}.
CC   -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC       the endoribonuclease activity. {ECO:0000250|UniProtKB:P33309}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BX284603; CAA85277.1; -; Genomic_DNA.
DR   PIR; T24256; T24256.
DR   RefSeq; NP_497842.1; NM_065441.4.
DR   AlphaFoldDB; P50444; -.
DR   SMR; P50444; -.
DR   BioGRID; 52565; 2.
DR   STRING; 6239.R74.6; -.
DR   EPD; P50444; -.
DR   PaxDb; P50444; -.
DR   PeptideAtlas; P50444; -.
DR   EnsemblMetazoa; R74.6.1; R74.6.1; WBGene00011280.
DR   GeneID; 187888; -.
DR   KEGG; cel:CELE_R74.6; -.
DR   UCSC; R74.6; c. elegans.
DR   CTD; 187888; -.
DR   WormBase; R74.6; CE01059; WBGene00011280; pelo-1.
DR   eggNOG; KOG2869; Eukaryota.
DR   GeneTree; ENSGT00390000016326; -.
DR   HOGENOM; CLU_023334_3_1_1; -.
DR   InParanoid; P50444; -.
DR   OMA; DDLWHLK; -.
DR   OrthoDB; 953123at2759; -.
DR   PhylomeDB; P50444; -.
DR   PRO; PR:P50444; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00011280; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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   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; 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   Cell cycle; Cell division; Cytoplasm; Endonuclease; Hydrolase; Meiosis;
KW   Metal-binding; Mitosis; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..381
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000143192"
SQ   SEQUENCE   381 AA;  42878 MW;  2B81A829B782FDCC CRC64;
     MKQFKRGIER DGTGFVVLMA EEAEDMWHIY NLIRIGDIIK ASTIRKVVSE TSTGTTSSQR
     VHTMLTVSVE SIDFDPGAQE LHLKGRNIEE NDIVKLGAYH TIDLEPNRKF TLQKTEWDSI
     DLERLNLALD PAQAADVAAV VLHEGLANVC LITPAMTLTR AKIDMTIPRK RKGFTSQHEK
     GLEKFYEAVS TAFMRHVNLQ VVKCVIVASR GFVKDAFMQH LIAHADANGK KFTTEQRAKF
     MLTHSSSGFK HALKEVLETP QVALRLADTK AQGEVKALNQ FLELMSTEPD RAFYGFNHVN
     RANQELAIET LLVADSLFRA QDIETRRKYV RLVESVREQN GKVHIFSSMH VSGEQLAQLT
     GCAAILRFPM PDLDDEPMDE N