ID   PELO_DANRE              Reviewed;         385 AA.
AC   Q7ZWC4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Protein pelota homolog;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN   Name=pelo;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2003) 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; BC049484; AAH49484.1; -; mRNA.
DR   RefSeq; NP_957430.1; NM_201136.1.
DR   AlphaFoldDB; Q7ZWC4; -.
DR   SMR; Q7ZWC4; -.
DR   STRING; 7955.ENSDARP00000072295; -.
DR   PaxDb; Q7ZWC4; -.
DR   Ensembl; ENSDART00000077829; ENSDARP00000072295; ENSDARG00000055477.
DR   GeneID; 394111; -.
DR   KEGG; dre:394111; -.
DR   CTD; 53918; -.
DR   ZFIN; ZDB-GENE-040426-1074; pelo.
DR   eggNOG; KOG2869; Eukaryota.
DR   GeneTree; ENSGT00390000016326; -.
DR   HOGENOM; CLU_023334_3_1_1; -.
DR   InParanoid; Q7ZWC4; -.
DR   OMA; DDLWHLK; -.
DR   OrthoDB; 953123at2759; -.
DR   PhylomeDB; Q7ZWC4; -.
DR   TreeFam; TF105733; -.
DR   PRO; PR:Q7ZWC4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 12.
DR   Bgee; ENSDARG00000055477; Expressed in somite and 27 other tissues.
DR   ExpressionAtlas; Q7ZWC4; baseline and differential.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; 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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Endonuclease; Hydrolase;
KW   Metal-binding; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000232838"
SQ   SEQUENCE   385 AA;  43081 MW;  AA75F54A20B1157A CRC64;
     MKLVHKDIEK DNAGQVTLIP DEAEDMWHTY NLLQVGDSLR ASTIRKVQTE SSTGSVGSSR
     VRTTLTLCVE TIDFDSQACQ LRVKGTNIQE NQYVKMGAYH TIELELNRKF TLAKKVWDSV
     VLDRIEQACD PAQKADVAAV VMQEGLANLV LVTPAMTLLR AKVEVTIPRK RKGSCTQHDK
     ALERFYEAVM QGILRHFNFD VVKCILVASP GFVKDQFISY LFKEAVRQDC KLLLENRSKF
     MVVHSSSGHK YSLKEVLCDP AVTARLSDTK AAGEVKALED FYKMLQQEPD RAFYGLAHVE
     RASEALAIDI LLISDTLFRH QDVATRGRYV RLVDNVKENG GTVRIFSSLH VSGEQLNQLS
     GVAAILRFPI ADVSEPEENS SSDED