ID   RF1_RHOJR               Reviewed;         359 AA.
AC   Q0SGN8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE            Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN   Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093};
GN   OrderedLocusNames=RHA1_ro01483;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC       translation in response to the peptide chain termination codons UAG and
CC       UAA. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR   EMBL; CP000431; ABG93298.1; -; Genomic_DNA.
DR   RefSeq; WP_011594475.1; NC_008268.1.
DR   AlphaFoldDB; Q0SGN8; -.
DR   SMR; Q0SGN8; -.
DR   STRING; 101510.RHA1_ro01483; -.
DR   EnsemblBacteria; ABG93298; ABG93298; RHA1_ro01483.
DR   KEGG; rha:RHA1_ro01483; -.
DR   PATRIC; fig|101510.16.peg.1502; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_11; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00093; Rel_fac_1; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004373; RF-1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00019; prfA; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..359
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263332"
FT   MOD_RES         238
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   359 AA;  38941 MW;  4D1F7E5AB8CB5C1C CRC64;
     MAGTTQPSAI DDILAEHAGL EQQLADPALH NDPSAARKAG KRFAELAPIM ATYAKLKSAQ
     DDLDAARELA ADDSSFAAEV PELEAQVLEL DKALTDLLAP RDPHDGDDVV LEVKSGEGGE
     ESALFASDLA RMYVRYAERH GWRVEILDAT VSDLGGYKDA TLSIKSKGDV RDGVWARLKF
     EGGVHRVQRV PVTESQGRVH TSAAGVLIYP EPEEVEEVQI DETDLRIDVY RSSGKGGQGV
     NTTDSAVRIT HLPTGIVVTC QNERSQLQNK ARAMQVLAAR LQAAAEEAAD AEASAGRQSQ
     VRTVDRSERI RTYNFPENRI TDHRIGFKSH NLDAVLDGEL DALLDALGKS DREARLAAE