ID   RF1_CERS4               Reviewed;         351 AA.
AC   Q3J2B6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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}; OrderedLocusNames=RHOS4_15000;
GN   ORFNames=RSP_2907;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000143; ABA79068.1; -; Genomic_DNA.
DR   RefSeq; WP_011337837.1; NZ_CP030271.1.
DR   RefSeq; YP_352969.1; NC_007493.2.
DR   AlphaFoldDB; Q3J2B6; -.
DR   SMR; Q3J2B6; -.
DR   STRING; 272943.RSP_2907; -.
DR   EnsemblBacteria; ABA79068; ABA79068; RSP_2907.
DR   KEGG; rsp:RSP_2907; -.
DR   PATRIC; fig|272943.9.peg.1844; -.
DR   eggNOG; COG0216; Bacteria.
DR   OMA; ISDHRVG; -.
DR   PhylomeDB; Q3J2B6; -.
DR   Proteomes; UP000002703; Chromosome 1.
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..351
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263331"
FT   MOD_RES         229
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   351 AA;  38595 MW;  9E3317FA5D122DCE CRC64;
     MVPMDRLLQI VRRFEFLEAR LSAGAAPAEI AALSREYAEL KPVVVEISAY RTALEDLAEA
     EAMLSDPEMR ALAEDEIPAL RARIPGMEQA LRLALLPKDA ADARPAILEI RPGTGGEEAA
     LFAGDLLRMY QRYAEGQGWR FELLDLAPSE LGGIREATAR VEGEGAFARL KYESGVHRVQ
     RVPETEAQGR IHTSAATVAV LPEAEEVDLE IPAADIRIDT MRSSGAGGQH VNTTDSAVRI
     THLPTGIIVT SSEKSQHRNR EIAMQVLRAR LYDLERQRLA DARSADRKAQ VGSGDRSERI
     RTYNFPQGRM TDHRINLTLY ALPQIMAGDL SEVISALTAH DQAARLAEME A