ID   RF1_RICAH               Reviewed;         355 AA.
AC   A8GNQ4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=A1C_03760;
OS   Rickettsia akari (strain Hartford).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=293614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hartford;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia akari.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000847; ABV75029.1; -; Genomic_DNA.
DR   RefSeq; WP_012149660.1; NC_009881.1.
DR   AlphaFoldDB; A8GNQ4; -.
DR   SMR; A8GNQ4; -.
DR   STRING; 293614.A1C_03760; -.
DR   EnsemblBacteria; ABV75029; ABV75029; A1C_03760.
DR   KEGG; rak:A1C_03760; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000006830; 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..355
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000004941"
FT   REGION          281..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..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;  39702 MW;  6C312A93ED76CA94 CRC64;
     MSFSDNLAKI LDKYDNLGKK LSSGIMGDEF VKASKEYAEL EDVVVKIKEY NKAKSELEEA
     NNFKLELGFD NATLAMIEDE IHILENSLPK LERAVKIALL PKDDADSKSA IIEVRAGSGG
     EEAALFAAVL FNMYQRYAEL KGWRFEILAI SDTGIGGYKE ASASIKGKDV FSKLKFESGV
     HRVQRVPETE SQGRIHTSAA TVAVLPEAEE VDIKIEDKDL RIDTYRASGA GGQHVNTTDS
     AVRITHIPTG ITVALQDEKS QHKNKAKALK ILRARIYEEE RRNKEQERAD SRRGQIGSGD
     RSERIRTYNF PQGRVSDHRI NLTLYKIDEV VKNGQLDEFI EALIAEDEAK KLSEI