ID   RF1_RICRO               Reviewed;         355 AA.
AC   B0BXT9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=RrIowa_0827;
OS   Rickettsia rickettsii (strain Iowa).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=452659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa;
RX   PubMed=18025092; DOI=10.1128/iai.00952-07;
RA   Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F.,
RA   Hackstadt T.;
RT   "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and
RT   avirulent Rickettsia rickettsii Iowa.";
RL   Infect. Immun. 76:542-550(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; CP000766; ABY72665.1; -; Genomic_DNA.
DR   RefSeq; WP_012150880.1; NC_010263.3.
DR   AlphaFoldDB; B0BXT9; -.
DR   SMR; B0BXT9; -.
DR   STRING; 452659.RrIowa_0827; -.
DR   EnsemblBacteria; ABY72665; ABY72665; RrIowa_0827.
DR   GeneID; 45539259; -.
DR   KEGG; rrj:RrIowa_0827; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000000796; 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_1000075511"
FT   REGION          282..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..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;  39730 MW;  9053808AA2A62BF8 CRC64;
     MRFSDNLAKI LDKYENLGNK LSSGIMGDEF VKASKEYAEL EDVVAKIKEY NKAKSELEEA
     NNFKLEVGLD NATLEMIEDE IYTLENSLPK LERAVKIALL PKDDADSKSA IIEVRAGSGG
     EEAALFAAVL FNMYQRYAEL KGWRFEILAI SDTGIGGYKE ASASIKGKDV FSKLKFESGV
     HRVQRVPETE SQGRIHTSAA TVAVLPEAEE VDIKIEDKDL RIDTYRASGA GGQHVNTTDS
     AVRITHIPTG ITVALQDEKS QHKNKAKALK ILRARIYEEE RRKKEQARAD SRRGQVGSGD
     RSERIRTYNF PQGRVSDHRI HLTLYKIDEV VKNGQLDEFV EALIADDEAK KLLEI