RF2_RALPJ
ID RF2_RALPJ Reviewed; 367 AA.
AC B2U8V1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000255|HAMAP-Rule:MF_00094};
DE Short=RF-2 {ECO:0000255|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000255|HAMAP-Rule:MF_00094}; OrderedLocusNames=Rpic_0895;
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 2 directs the termination of
CC translation in response to the peptide chain termination codons UGA and
CC UAA. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00094}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001068; ACD26045.1; -; Genomic_DNA.
DR AlphaFoldDB; B2U8V1; -.
DR SMR; B2U8V1; -.
DR STRING; 402626.Rpic_0895; -.
DR EnsemblBacteria; ACD26045; ACD26045; Rpic_0895.
DR KEGG; rpi:Rpic_0895; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_220733_0_0_4; -.
DR OMA; YVFHPYQ; -.
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_00094; Rel_fac_2; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004374; PrfB.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
DR TIGRFAMs; TIGR00020; prfB; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methylation; Protein biosynthesis.
FT CHAIN 1..367
FT /note="Peptide chain release factor 2"
FT /id="PRO_1000093552"
FT MOD_RES 254
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 367 AA; 41167 MW; 769765D2E8B46C5D CRC64;
MEAERLNAIQ NTLADLKSRA DDLRRYLDYD VKSERLVEVD KELENPEVWN DPKRAQELGR
EKKSLETVVL ALTKLDEDLT GAAELFELAR EEGDDETIEA IEADTAGMRA IVEDMEFRRM
FSGPMDAANC FIDIQAGAGG TEACDWASML LRQYLKYCER KGFKTEVLEE SEGDVAGIKS
ASIKVEGEYA FGFLRTETGV HRLVRKSPFD SAGGRHTSFS SIFVYPEVDD SIEIEVNPAD
LRVDTYRASG AGGQHINKTD SAVRITHIPT GIVVQCQNDR SQHRNRAEAM TMLKSRLYEH
ELRKRQAAAD AQEAAKTDVG WGHQIRSYVL DQSRIKDLRT NVEISNTQKV LDGDLDPFIQ
ASLKQGV