ID   RF1_BIFLO               Reviewed;         362 AA.
AC   Q8G3P5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=BL1712;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014295; AAN25496.1; -; Genomic_DNA.
DR   RefSeq; NP_696860.1; NC_004307.2.
DR   RefSeq; WP_007052437.1; NC_004307.2.
DR   AlphaFoldDB; Q8G3P5; -.
DR   SMR; Q8G3P5; -.
DR   STRING; 206672.BL1712; -.
DR   EnsemblBacteria; AAN25496; AAN25496; BL1712.
DR   GeneID; 66505793; -.
DR   KEGG; blo:BL1712; -.
DR   PATRIC; fig|206672.9.peg.1765; -.
DR   HOGENOM; CLU_036856_0_1_11; -.
DR   OMA; ISDHRVG; -.
DR   PhylomeDB; Q8G3P5; -.
DR   Proteomes; UP000000439; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..362
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263237"
FT   MOD_RES         240
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   362 AA;  40054 MW;  AA6EA17227BBFAA5 CRC64;
     MADEQFPAAA TALEEYQSIE EQMASPEVVS NPDKLRKLGR RHAELGAIVG AYKAWLQVKD
     DLAAAQEMAG EDADFAEEAK RLEDELPGVE EKLRTALIPR DPDDARDTIM EIKAGTGGEE
     AALFAGDLLR MYTRYAEKRG WSVNVQSENT TELGGVKDVQ IAIRAKGTPA PEDGVWASMK
     YEGGVHRVQR IPVTESQGRI QTSAAGVIVF PEADEDDDEI EIDPKDLKID IFMSSGPGGQ
     SVNTTYSAVR MTHLPTGITV NMQDEKSQIQ NRAAALRVLK SRLLAMKHEQ EAAEAADMRH
     SQVRSLDRSE RIRTYNFPEN RIVDHRTNYK AYNLDAVLDG DLQAVIDSDI QADEADRLAN
     QK