ID A0A1H9WD78_9CORY Unreviewed; 366 AA.
AC A0A1H9WD78;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05661109_02673 {ECO:0000313|EMBL:SES31774.1};
OS Corynebacterium cystitidis DSM 20524.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121357 {ECO:0000313|EMBL:SES31774.1, ECO:0000313|Proteomes:UP000198929};
RN [1] {ECO:0000313|EMBL:SES31774.1, ECO:0000313|Proteomes:UP000198929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20524 {ECO:0000313|EMBL:SES31774.1,
RC ECO:0000313|Proteomes:UP000198929};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOGQ01000020; SES31774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9WD78; -.
DR STRING; 1121357.SAMN05661109_02673; -.
DR Proteomes; UP000198929; 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 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}.
FT DOMAIN 240..256
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 276..303
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 247
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 366 AA; 40995 MW; 21080B3C936C747B CRC64;
MQPETSSAIE HLDATLTTIE KVMDLDELDM RVRELEQQAA DPSLWDDPDH AQQVTTELSN
VQARLRKVRD LRTRIDDLPV MYELSEEEGD TSVAEDELAE VTKLIDALEV TTMLSGEYDE
REAMINIRSG AGGVDAADWA EMLMRMYIRW AEKNGHKVDV YDISYAEEAG IKSATFVVHG
DYMYGQLSVE QGAHRLVRIS PFDNQGRRQT SFAEVEVLPV VEKTDSIDIP DSDIRVDVFR
SSGPGGQSVN TTDSAVRITH LPTNIVVSCQ NEKSQIQNKA SALAVLQSKL LELKRQEEKA
EMDALGAGGN ASWGNQMRSY VLHPYQMVKD LRTDYEVSDP QKVLDGDIDG FLEAGIRWRM
AEEASH
//
