ID   PELO_XENLA              Reviewed;         383 AA.
AC   Q5U567;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Protein pelota homolog;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN   Name=pelo;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cotranslational quality control factor involved in the No-Go
CC       Decay (NGD) pathway. Required for 48S complex formation from 80S
CC       ribosomes and dissociation of vacant 80S ribosomes. Recognizes stalled
CC       ribosomes and promotes dissociation of elongation complexes assembled
CC       on non-stop mRNAs; this triggers endonucleolytic cleavage of the mRNA,
CC       a mechanism to release non-functional ribosomes and to degrade damaged
CC       mRNAs as part of the No-Go Decay (NGD) pathway. Upon mitochondrial
CC       damage is recruited to the ribosome/mRNA-ribonucleoprotein complex
CC       associated to mitochondrial outer membrane thereby enabling the
CC       recruitment of autophagy receptors and induction of mitophagy.
CC       {ECO:0000250|UniProtKB:Q9BRX2}.
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 {ECO:0000250}.
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; BC084817; AAH84817.1; -; mRNA.
DR   RefSeq; NP_001088486.1; NM_001095017.2.
DR   AlphaFoldDB; Q5U567; -.
DR   SMR; Q5U567; -.
DR   PRIDE; Q5U567; -.
DR   DNASU; 495353; -.
DR   GeneID; 495353; -.
DR   KEGG; xla:495353; -.
DR   CTD; 495353; -.
DR   Xenbase; XB-GENE-5901616; pelo.L.
DR   OrthoDB; 953123at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 495353; Expressed in testis and 20 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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   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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Endonuclease; Hydrolase;
KW   Metal-binding; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..383
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000232839"
SQ   SEQUENCE   383 AA;  43147 MW;  A5F2DD107EC6420A CRC64;
     MKLIRKDIEK DNAGQVTLIP EEAEDMWHTY NLLHVGDSLQ ASTIRKVQTE SSTGSVGSNR
     VRTTLTICVE TIDFDSQACQ LRVKGINIQE NQYVKMGAYH TIELEPNRKF TLAKKQWDSI
     VLERIEQACD PAFSADVAAV VMQEGLAHIC LVTPSMTLLR AKIETSIPRK RRGNCTQHEK
     ALEKFYEQVM QGILRHINFD VVKVVLVASP GFVREQFCEF LFLRAVKQDL KILLENRGKF
     LQVHSSSGRK YSLTEVLCDP AVTARLSDTK AACEIKALGD FYKMLQHEPD RAFYGIKQVE
     KANEALAVDT LLVTDELFRH QDVPTRTRYV RLVDSVKDNG GTVRIFSSLH VSGEQLNQLT
     GVAAILRFPV ADLSDEESSS DED