RF1_LEPIN
ID RF1_LEPIN Reviewed; 354 AA.
AC Q8F9S6;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=LA_0114;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; AE010300; AAN47313.1; -; Genomic_DNA.
DR RefSeq; NP_710295.1; NC_004342.2.
DR RefSeq; WP_000567183.1; NC_004342.2.
DR AlphaFoldDB; Q8F9S6; -.
DR SMR; Q8F9S6; -.
DR STRING; 189518.LA_0114; -.
DR EnsemblBacteria; AAN47313; AAN47313; LA_0114.
DR GeneID; 61143457; -.
DR KEGG; lil:LA_0114; -.
DR PATRIC; fig|189518.3.peg.117; -.
DR HOGENOM; CLU_036856_0_1_12; -.
DR InParanoid; Q8F9S6; -.
DR OMA; ISDHRVG; -.
DR Proteomes; UP000001408; Chromosome I.
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..354
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177692"
FT MOD_RES 230
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 354 AA; 40099 MW; 779A91ACCC997A59 CRC64;
MIDRLEKIQE KYLRISEELN QAKDPSSLKN LYKERSRLTP LYLKVEEYLK IYKDRKDAEE
LIQSEKDEEM HSMLKEEIRE ANLKLETLER EFEILLLPPD PNSGKNILVE IRAGTGGEEA
GLFVADLFRM YSKFADKQKI KTEIIDSSPT GIGGLKEIIF ALEDDRAYDL FKFEGGTHRV
QRIPSTESGG RIHTSAVTVA VLPEADEEEV QINESDLRID VYRSSGAGGQ HVNTTDSAVR
ITHIPTGVVV ACQDEKSQHK NKAKALRILS ARILEKQAED KKQASDAIKK QMIGSGDRSE
RVRTYNFPQG RCTDHRIGFT SHNLSAIMEG DLDELIGALT EEDRVRKISE TQTH