ID   RF1_HYDS0               Reviewed;         356 AA.
AC   B4U955;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=HY04AAS1_0980;
OS   Hydrogenobaculum sp. (strain Y04AAS1).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum;
OC   unclassified Hydrogenobaculum.
OX   NCBI_TaxID=380749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y04AAS1;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001130; ACG57666.1; -; Genomic_DNA.
DR   RefSeq; WP_012514022.1; NC_011126.1.
DR   AlphaFoldDB; B4U955; -.
DR   SMR; B4U955; -.
DR   STRING; 380749.HY04AAS1_0980; -.
DR   EnsemblBacteria; ACG57666; ACG57666; HY04AAS1_0980.
DR   KEGG; hya:HY04AAS1_0980; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_0; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
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.
FT   CHAIN           1..356
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093464"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   356 AA;  40674 MW;  816B89B7AA8F1078 CRC64;
     MLPKNFLEKI QDIEQKYAQT EEKLASLDIT KDADTYKALS KDLKELSYIH ELYKDYNKIL
     KDIEDTKELL KDKDLRELAE KELENLNTKL LQKEKELINV LTPKDANDSK NVILEIRAGA
     GGEEAALFAA DLLRMYQRYA ERKGWKFNIL EANKTGLGGY KEVIVSIEGK NVYSHLKYES
     GVHRVQRVPI TESGGRIHTS TITVAVLPEA DETDVVINPQ DLRIETFRAS GAGGQYVNTT
     ESAVRITHIP TGISISCQDE RSQLQNKLKA MRILYARLKD FYEKQKKEET DKERKEQVGT
     GERSEKIRTY NFSQNRVTDH RINLTLHKLQ DVLDGDLDDI ISSLQAKELE EKLASA