RF1_RALPJ
ID RF1_RALPJ Reviewed; 360 AA.
AC B2UDM7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Rpic_3146;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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; CP001068; ACD28268.1; -; Genomic_DNA.
DR RefSeq; WP_012436504.1; NC_010682.1.
DR AlphaFoldDB; B2UDM7; -.
DR SMR; B2UDM7; -.
DR STRING; 402626.Rpic_3146; -.
DR EnsemblBacteria; ACD28268; ACD28268; Rpic_3146.
DR KEGG; rpi:Rpic_3146; -.
DR PATRIC; fig|402626.5.peg.4286; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_4; -.
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..360
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000093493"
FT REGION 283..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 40002 MW; 7A60BCFA19403E40 CRC64;
MKPSMLSKLD QLAERIVEIN ALLAREDATA NLDQYRKLTR EHAELEPVVA QFAAWKQAEE
DIATAQELAA DPDMKAFAED ELRAARERME SLEGELQRLL LPKDPNDHRN IFVEIRAGTG
GDESALFAGD LLRMYTRYAE RQRWQVEIVS ESPSDLGGYK EVIARLVGEG AYSRLKFESG
GHRVQRVPAT EAQGRIHTSA CTVAVMPEAD ALADIQINPA DLRIDTFRAS GAGGQHINKT
DSAVRITHLP TGLVVECQDD RSQHRNKDRA MQVLAARLKD RQEREAQAKE ASARKSLIGS
GDRSDRIRTY NFPQGRVTDH RINLTLYKID AIMDGDIDEL VGALAAEHQA EQLAALGEDA