ID   RF1_RICM5               Reviewed;         361 AA.
AC   A8F1S1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=RMA_0703;
OS   Rickettsia massiliae (strain Mtu5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=416276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mtu5;
RX   PubMed=17916642; DOI=10.1101/gr.6742107;
RA   Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT   "Lateral gene transfer between obligate intracellular bacteria: evidence
RT   from the Rickettsia massiliae genome.";
RL   Genome Res. 17:1657-1664(2007).
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; CP000683; ABV84857.1; -; Genomic_DNA.
DR   RefSeq; WP_012152832.1; NC_009900.1.
DR   AlphaFoldDB; A8F1S1; -.
DR   SMR; A8F1S1; -.
DR   PRIDE; A8F1S1; -.
DR   EnsemblBacteria; ABV84857; ABV84857; RMA_0703.
DR   KEGG; rms:RMA_0703; -.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000001311; 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.
FT   CHAIN           1..361
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000057618"
FT   REGION          280..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..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   361 AA;  40331 MW;  ACFED61DD8105B23 CRC64;
     MRFSDNLAKI LDKYENLGNK LSSGIMGDEF VKASKEYAEL EDVVAKIKEY NKAKSELEEA
     NNFKLEVGLD NATLEMIEDE IHTLENSLPK LERAVKIALL PKDDADSKSA IIEVRAGSGG
     EEAALFAAVL FNMYQRYAEL KGWRFEILAI SDTGIGGYKE ASASIKGKDV FSKLKFESGV
     HRVQRVPETE SQGRIHTSAA TVAVLPEAEE VDIQIEDKDL RIDTYRASGA GGQHVNTTDS
     AVRITHIPTG ITVALQDEKS QHKNKAKALK ILRARIYEEE RRKKEQERAD SRRGQVGSGD
     RSERIRTYNF PQGRVSDHRI NLTLYKIDEV VKNGQLDEFV EALIADDEAK KLLGIYSKNT
     A