ID   RF1_FRATH               Reviewed;         361 AA.
AC   Q2A1Q0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=FTL_1721;
OS   Francisella tularensis subsp. holarctica (strain LVS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=376619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVS;
RA   Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA   Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA   Garcia E.;
RT   "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT   Strain).";
RL   Submitted (MAR-2006) 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; AM233362; CAJ80160.1; -; Genomic_DNA.
DR   RefSeq; WP_003017177.1; NZ_CP009694.1.
DR   AlphaFoldDB; Q2A1Q0; -.
DR   SMR; Q2A1Q0; -.
DR   KEGG; ftl:FTL_1721; -.
DR   OMA; ISDHRVG; -.
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_0000263275"
FT   REGION          287..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         237
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   361 AA;  40402 MW;  FE634A4560245388 CRC64;
     MKDSIKAKLQ SLIERHEEVS ALLSEAGIIS DQNKFRDLSK EYSHLEPIVK AFKEYTQALE
     DKQAAYEMLN EKDAELVEMA KEELKLANEA IEKLESELQI FLLPRDPNDD ANVFLEIRAG
     TGGDEASIFS GDLFKMYSKY AEQRGWKIEV ISASEGEHGG YKEIISRIYG DGVYSQLKFE
     SGAHRVQRVP ATESQGRIHT SACTVAVMPE ADEVEGIDIN PADIKVDTFR ASGAGGQHVN
     KTDSAIRITH IPTGVVVECQ DQRSQHKNRA AAMSMLKSKL LQAEIDKQQK EQSDTRKSLV
     GSGDRSERIR TYNYPQGRVT DHRINLTLYK LDEVMEGSLD SIIQPLVLEH QADLLATMSD
     E