RF1_LIMRJ
ID RF1_LIMRJ Reviewed; 360 AA.
AC B2G676;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=LAR_0442;
OS Limosilactobacillus reuteri (strain JCM 1112) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557433;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 1112;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(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; AP007281; BAG24958.1; -; Genomic_DNA.
DR AlphaFoldDB; B2G676; -.
DR SMR; B2G676; -.
DR KEGG; lrf:LAR_0442; -.
DR HOGENOM; CLU_036856_0_1_9; -.
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..360
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000093469"
FT MOD_RES 236
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 41027 MW; B571F4972CCD0EAB CRC64;
MEEIFDKLQA VADRYDELNE LISDPEVIAD SQRFMKLSKE EGSLRETVEK YNQYKKVTQT
ISDDEELLRE TNDDDLTALT KEELAEAREE QAQLEKELEV LLIPKDPNDD KNIIMEIRGA
AGGDEASLFA ADLYNMYLRY AEKQGWKVEV VDRNETEVGG FKEIALMITG DKVYSKLKFE
NGAHRVQRVP VTESAGRVHT STATVGVMPE AEDVDVDIDP KDIRVDVYRS SGAGGQHVNK
TSSAVRMTHL PTGIVVAMQD ERSQQQNRAK AMRILKSRVY DYYQQQEQSA YDQKRKDAIG
TGDRSERIRT YNYPQNRVTD HRIGLTLNKL DKIMAGDLDE IIEALIVADQ TQKLEQLRNE