ID A0A316TRW0_9ACTN Unreviewed; 371 AA.
AC A0A316TRW0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 08-OCT-2025, entry version 24.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|HAMAP-Rule:MF_00094, ECO:0000256|NCBIfam:TIGR00020};
DE Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094,
GN ECO:0000313|EMBL:PWN02376.1};
GN ORFNames=DJ010_14855 {ECO:0000313|EMBL:PWN02376.1};
OS Nocardioides silvaticus.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2201891 {ECO:0000313|EMBL:PWN02376.1, ECO:0000313|Proteomes:UP000245507};
RN [1] {ECO:0000313|EMBL:PWN02376.1, ECO:0000313|Proteomes:UP000245507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2018079 {ECO:0000313|EMBL:PWN02376.1,
RC ECO:0000313|Proteomes:UP000245507};
RA Li C., Wang G.;
RT "Nocardioides silvaticus genome.";
RL Submitted (MAY-2018) 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|ARBA:ARBA00002613, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWN02376.1}.
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DR EMBL; QGDD01000006; PWN02376.1; -; Genomic_DNA.
DR RefSeq; WP_109695083.1; NZ_QGDD01000006.1.
DR AlphaFoldDB; A0A316TRW0; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000245507; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR FunFam; 3.30.160.20:FF:000004; Peptide chain release factor 1; 1.
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:SF3; CLASS I PEPTIDE CHAIN RELEASE FACTOR; 1.
DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00094};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00094};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Reference proteome {ECO:0000313|Proteomes:UP000245507}.
FT DOMAIN 244..260
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 371 AA; 40748 MW; E2391F4C00490786 CRC64;
MAGPEYDTEI KQLVATMHTI EQVLDLPAMR AEIDDLGVQV AAPDLWDDQA NATRVTGRLS
ALQGQVERFE ALKGRIDDLG VLVELAQEEQ DADSLAEAEA ELGKIKKAVE ALEVRTLLSG
EYDEREAIVT IRSGAGGVDA ADFAEMLMRM YTRWAERNNY PVEVYDVSYA EEAGIKSAEF
AIHAPYGYGT LSVEAGTHRL VRISPFDNQG RRQTSFAAVE VVPQLEQTDE IEVDENEVRV
DVFRSGGPGG QSVNTTDSAV RLTHIPTGIV VSCQNEKSQL QNKAAAMIVL KAKLLARKKA
EEAALKKDLK GDVAASWGDQ MRNYVLNPYQ IVKDLRTGYE SGNPQAVFDG DLDDFLEAGI
RWRRGAEKAD A
//
