ID   RF1_FINM2               Reviewed;         355 AA.
AC   B0S2B6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=FMG_1088;
OS   Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS   (Peptostreptococcus magnus).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=334413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX   PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA   Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA   Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT   "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT   pathogen.";
RL   DNA Res. 15:39-47(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; AP008971; BAG08506.1; -; Genomic_DNA.
DR   RefSeq; WP_002840294.1; NC_010376.1.
DR   AlphaFoldDB; B0S2B6; -.
DR   SMR; B0S2B6; -.
DR   STRING; 334413.FMG_1088; -.
DR   EnsemblBacteria; BAG08506; BAG08506; FMG_1088.
DR   KEGG; fma:FMG_1088; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_9; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000001319; 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..355
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093456"
FT   REGION          283..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         233
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   355 AA;  40472 MW;  DFDF355CCFBA8534 CRC64;
     MFENLDSVVD KFKDLEVKVA DPEVIADMEN WTKLMKEHAD LEPVVNKYLS YKDNLKNLEE
     DKELLGTTGD SEMEELLKDE ISTLEEQIEK DQEELKILLL PKDPNDEKNV FIEIRAGAGG
     DEAGLFAGEL LRMYQMYSDK KHWTTEIMDI QQQGVGGIKE VVMMVKGKGA YSRLKYESGV
     HRVQRVPQTE SSGRIHTSTA TVAVLPEAED VDVKIEQKDL RIDVFRASGN GGQCVNTTDS
     AVRITHIPTG LVVTCQDEKS QIKNKDKAMK VLKSRLYDLM EEEKNKDRAD ARKSQVGTGD
     RSERIRTYNF PQGRITDHRI NKTIFQLQNF LDGDIEEMID DLTSYDQAEK LKMMN