ID   RF1_RICPR               Reviewed;         355 AA.
AC   Q9ZD21;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Peptide chain release factor 1;
DE            Short=RF-1;
GN   Name=prfA; OrderedLocusNames=RP529;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; AJ235272; CAA14978.1; -; Genomic_DNA.
DR   PIR; H71656; H71656.
DR   RefSeq; NP_220902.1; NC_000963.1.
DR   RefSeq; WP_004597801.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZD21; -.
DR   SMR; Q9ZD21; -.
DR   STRING; 272947.RP529; -.
DR   EnsemblBacteria; CAA14978; CAA14978; CAA14978.
DR   GeneID; 57569651; -.
DR   KEGG; rpr:RP529; -.
DR   PATRIC; fig|272947.5.peg.537; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000002480; 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_0000177731"
FT   REGION          280..310
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:0000250"
SQ   SEQUENCE   355 AA;  39895 MW;  D8E3D4BAE83C67F5 CRC64;
     MSFSDNLVKI LDKYENLGKK LSSGIIGDEF VKASKEYAEL EDVVVKIKQY NKAKSELEEA
     NNFRLEMALD NATLEMIDNE IHTLENLLPK LERAVRISLL PKDEADSKSA IIEVRAGSGG
     EEAALFAAVL FNMYQRYSEF KGWRFEILAI SDTGIGGYKE ASASIKGKDV FSKLKFESGV
     HRVQRIPETE SQGRIHTSAA TVAVLPEAEG IDIKIEDKDL RIDTYRASGA GGQHVNTTDS
     AVRITHIPTG ITVALQDEKS QHKNKAKALK ILRARLYEEK RRQKEQERSD SRRGQVGSGD
     RSERIRTYNF PQGRVSDHRI NLTLYKIDEV VKHGQLDEFI EALIANDEAK KLSEL