ID A0A411YC50_9ACTN Unreviewed; 357 AA.
AC A0A411YC50;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|HAMAP-Rule:MF_00094};
DE Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094};
GN ORFNames=ER308_03925 {ECO:0000313|EMBL:QBI18780.1};
OS Egibacter rhizosphaerae.
OC Bacteria; Actinomycetota; Nitriliruptoria; Egibacterales; Egibacteraceae;
OC Egibacter.
OX NCBI_TaxID=1670831 {ECO:0000313|EMBL:QBI18780.1, ECO:0000313|Proteomes:UP000291469};
RN [1] {ECO:0000313|EMBL:QBI18780.1, ECO:0000313|Proteomes:UP000291469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGI 80759 {ECO:0000313|EMBL:QBI18780.1,
RC ECO:0000313|Proteomes:UP000291469};
RA Chen D.-D., Tian Y., Jiao J.-Y., Zhang X.-T., Zhang Y.-G., Zhang Y.,
RA Xiao M., Shu W.-S., Li W.-J.;
RT "Egibacter rhizosphaerae EGI 80759T.";
RL Submitted (JAN-2019) 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:0000256|HAMAP-Rule:MF_00094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2. {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00094}.
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DR EMBL; CP036402; QBI18780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411YC50; -.
DR KEGG; erz:ER308_03925; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000291469; 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 Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 1.20.58.410; Release factor; 1.
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 NCBIfam; TIGR00020; prfB; 1.
DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 1.
DR PANTHER; PTHR43116:SF3; RF_PROK_I DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094};
KW Reference proteome {ECO:0000313|Proteomes:UP000291469}.
FT DOMAIN 223..239
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 50..93
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 230
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 357 AA; 39948 MW; 692669C7A087F42A CRC64;
MFDVDGKRRR LTELQGEAGD PALWDDQARA QRVMTELRRL EDDLGRYDAF AQKLADLETL
EQLAREENDE DAAVEVAQGV AALEREIAEL ELRVLLSGEY DHRDGVVTVH AGAGGTDSQD
WAEMLQRMLL RWCEHRGFGV DVHDVQHGDE AGIRSATFTV HGDRAYGLLQ AERGVHRLVR
ISPFDSQKRR HTAFASVDVI PVFEAVDDHV EVPEEELRID TFRSSGPGGQ SVNTTDSAVR
INHLPTGIVV QCQDQKSQLQ NKTVAMNLLK AKLAERARAE RQAEIDAVRG EQADVAWGSQ
IRSYVLHPYQ MVKDLRTGHE TGNTDAVLDG DLDAFIEAFL QWKARGEQQE RVGEGHV
//
