ID   RF1_OCEIH               Reviewed;         356 AA.
AC   Q8EM60;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=OB2998;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC14954.1; -; Genomic_DNA.
DR   RefSeq; WP_011067394.1; NC_004193.1.
DR   AlphaFoldDB; Q8EM60; -.
DR   SMR; Q8EM60; -.
DR   STRING; 221109.22778686; -.
DR   PRIDE; Q8EM60; -.
DR   EnsemblBacteria; BAC14954; BAC14954; BAC14954.
DR   KEGG; oih:OB2998; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_9; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   PhylomeDB; Q8EM60; -.
DR   Proteomes; UP000000822; 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..356
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000177717"
FT   MOD_RES         233
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   356 AA;  40497 MW;  D6F672842002D64A CRC64;
     MLDRLQSLED RYNKLNEMLS DPEVINDSKK LREYSKEQSG LEDVVQAYRE YKEVTEQLND
     AKEMMEDKLD DEMYEMVKAE IAELNGRKEE LESSMKILLL PKDPNDDKNV FMEIRGAAGG
     DEAALFAGDL YRMYSRYAEH QGWKIDVMEA SSTGVGGYKE VIFMINGSDV YSKLKYENGA
     HRVQRVPETE SGGRIHTSTA TVAVLPEAEE VEVEVHDKDI RVDTFASSGP GGQSVNTTMS
     AVRLTHVPTG IVVSIQDEKS QIKNKEKAMK VLRARIYDKF QQEAQAEYDE NRKSAVGSGD
     RSERIRTYNF PQNRVTDHRI GLTIQKLDQI MQGKLDEFID ALVMEEQTNK LEQIGE