ID   RF1_RUBXD               Reviewed;         364 AA.
AC   Q1AVG5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Rxyl_1652;
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) 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; CP000386; ABG04613.1; -; Genomic_DNA.
DR   RefSeq; WP_011564630.1; NC_008148.1.
DR   AlphaFoldDB; Q1AVG5; -.
DR   SMR; Q1AVG5; -.
DR   STRING; 266117.Rxyl_1652; -.
DR   PRIDE; Q1AVG5; -.
DR   EnsemblBacteria; ABG04613; ABG04613; Rxyl_1652.
DR   KEGG; rxy:Rxyl_1652; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_11; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   PhylomeDB; Q1AVG5; -.
DR   Proteomes; UP000006637; 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..364
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263342"
FT   MOD_RES         237
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   364 AA;  40789 MW;  02A0793AE8B75617 CRC64;
     MDEQVVKLAK ETVARYRELT EELSDPAIFN DQRRYAEVAR EHSRMRRGAE LSERFLEALR
     EEREARELIP AAESAEEREF FAGEAREAGR RAGELAEEIR SELIDRDPND DKDVILEIRA
     GTGGDEAALF AGDLYEMYAR YADRLGFRHR VLDASPAEVG GYKEIIVEIE GDGAYSVFKH
     EGGTHRVQRV PKTESQGRIH TSTATVAVLP EAEEVEVEIN PNDLEIDVYR SSGPGGQSVN
     TTDSAVRITH KPTGLVVTCQ NEKSQLQNKE QALRILRSRL LEREMRERQE REGQMRLAQF
     GSGDRSAKIR TYNFPQGRIT DHRVGLTVHN LEAVLGGELE EFTKALAAKE RADRLAASAT
     GSPG