ID   RF1_LEPBL               Reviewed;         354 AA.
AC   Q056R9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=LBL_0042;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L550;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000348; ABJ77676.1; -; Genomic_DNA.
DR   RefSeq; WP_011669162.1; NC_008508.1.
DR   AlphaFoldDB; Q056R9; -.
DR   SMR; Q056R9; -.
DR   KEGG; lbl:LBL_0042; -.
DR   HOGENOM; CLU_036856_0_1_12; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
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..354
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000004908"
FT   REGION          282..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         230
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   354 AA;  39997 MW;  90F8DBCC121124CD CRC64;
     MIDRLEKIQE KYLRISEELN SAKDPSSLKS LYKERSRLTP LYLKVEEYLK IYKDKKDAEE
     LIPSEKDEEM HSMLKEEIRR ASKKLEELEK ELEILLLTPD PNSGKNILVE IRAGTGGEEA
     GLFVADLFRM YSKFADKQKI KSEIIDSAPT GIGGLKEIIF ALEDERAYDL FKFEGGTHRV
     QRIPSTESGG RIHTSAVTVA VLPEADEEEI EINENDLRID VYRSSGAGGQ HVNTTDSAVR
     ITHIPTGVVV ACQDEKSQHK NKAKALRILS ARILEKQTED KKQASDAIKK QMIGSGDRSE
     RVRTYNFPQG RCTDHRIGFT SHNLSAIMEG DLEELIGALT EEDRARKISE TQVH