ID   PELO_CHICK              Reviewed;         385 AA.
AC   Q5ZK01;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Protein pelota homolog;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN   Name=PELO; ORFNames=RCJMB04_14b4;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720283; CAG31942.1; -; mRNA.
DR   RefSeq; NP_001026763.1; NM_001031592.1.
DR   AlphaFoldDB; Q5ZK01; -.
DR   SMR; Q5ZK01; -.
DR   BioGRID; 688593; 1.
DR   PaxDb; Q5ZK01; -.
DR   GeneID; 430689; -.
DR   KEGG; gga:430689; -.
DR   CTD; 53918; -.
DR   VEuPathDB; HostDB:geneid_430689; -.
DR   InParanoid; Q5ZK01; -.
DR   OrthoDB; 953123at2759; -.
DR   PhylomeDB; Q5ZK01; -.
DR   PRO; PR:Q5ZK01; -.
DR   Proteomes; UP000000539; Unplaced.
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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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;
KW   Translation regulation.
FT   CHAIN           1..385
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000232837"
SQ   SEQUENCE   385 AA;  43507 MW;  D950139BCD1B41C2 CRC64;
     MKLVRKDLEK DNAGQVTLIP EEPEDMWHTY NLLQVGDSLR ASTIRKVQTE SSTGSVGSNR
     IRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV
     VLERIEQACD PAWNADVAAV VMQEGLAHVC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR
     ALERFYEQVV QAIQRHINFE VVKCVLVASP GFVREQFCDY MFQQAVKTDN KLLLENRSKF
     LQVHSSSGHK YVLKEALCDP AVTSRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKHVE
     KANEAMAIDT LLISDELFRH QDVATRARYV KLVDSVRENM GTVRIFSSLH VSGEQLGQLT
     GVAAILRFPV AELSDQEDES SSEED