ID   RF1_BIFLD               Reviewed;         362 AA.
AC   B3DR51;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=BLD_1889;
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=205913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A;
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(2008).
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; CP000605; ACD99334.1; -; Genomic_DNA.
DR   RefSeq; WP_010080980.1; NZ_AABM02000004.1.
DR   AlphaFoldDB; B3DR51; -.
DR   SMR; B3DR51; -.
DR   EnsemblBacteria; ACD99334; ACD99334; BLD_1889.
DR   KEGG; blj:BLD_1889; -.
DR   HOGENOM; CLU_036856_0_1_11; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000002419; 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.
FT   CHAIN           1..362
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093425"
FT   MOD_RES         240
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   362 AA;  40112 MW;  04BE6E72E9A52AA4 CRC64;
     MADEQFPAAA TALEEYQSIE EQMASPEVVS NPDKLRKLGR RHAELGAIVD 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