RF2_EXIS2
ID RF2_EXIS2 Reviewed; 366 AA.
AC B1YLH0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Exig_2425;
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-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}.
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DR EMBL; CP001022; ACB61875.1; -; Genomic_DNA.
DR RefSeq; WP_012371291.1; NC_010556.1.
DR AlphaFoldDB; B1YLH0; -.
DR SMR; B1YLH0; -.
DR STRING; 262543.Exig_2425; -.
DR EnsemblBacteria; ACB61875; ACB61875; Exig_2425.
DR KEGG; esi:Exig_2425; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_036856_6_0_9; -.
DR OMA; YVFHPYQ; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000001681; Chromosome.
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; Reference proteome.
FT CHAIN 1..366
FT /note="Peptide chain release factor 2"
FT /id="PRO_1000093539"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 366 AA; 42141 MW; 18EC270620C9E9B7 CRC64;
MELAEIRNTA EWMEKKLDEY KASLDLETKI SRIEELENEM TYPDFWNNQE SAQKVIDESN
GLKAMVDKYQ HLADGHENIV LTYELIKEEP DVELQEELES ELGDIKKKFD EFELQILLNG
EYDANNAILE LHPGAGGTES QDWASMLLRM YQRFCDKQGW KVETMDYQPG DEAGVKSVTL
RIQGHNAYGY LKAEKGIHRL VRISPFDSSG RRHTSFVSCD VMPEFNDDID IEIRTEDLRV
DTYRASGAGG QHINTTDSAV RITHVPTGVV VSCQQERSQI KNREAAMKML KAKLYQREIE
EKQKKLDEIR GEKSDIAWGS QIRSYVFHPY SMVKDHRTNY EVGNTQGAMD GDIMGFIDAY
LRLMNM