ID A0A3G3K0Q9_9BACL Unreviewed; 372 AA.
AC A0A3G3K0Q9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|ARBA:ARBA00019192, 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 ECO:0000313|EMBL:AYQ74125.1};
GN ORFNames=EAV92_17085 {ECO:0000313|EMBL:AYQ74125.1};
OS Cohnella candidum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=2674991 {ECO:0000313|EMBL:AYQ74125.1, ECO:0000313|Proteomes:UP000269097};
RN [1] {ECO:0000313|EMBL:AYQ74125.1, ECO:0000313|Proteomes:UP000269097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=18JY8-7 {ECO:0000313|EMBL:AYQ74125.1,
RC ECO:0000313|Proteomes:UP000269097};
RA Srinivasan S., Kim M.K.;
RT "Genome Sequence of Cohnella sp.";
RL Submitted (OCT-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}.
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DR EMBL; CP033433; AYQ74125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G3K0Q9; -.
DR KEGG; coh:EAV92_17085; -.
DR Proteomes; UP000269097; 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:UP000269097}.
FT DOMAIN 246..262
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 64..94
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 253
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 372 AA; 42337 MW; 12014B55B69EA1CD CRC64;
MSELDVSVKQ DLRECAKRLQ QLRGSLDLDL KREQIENYEV KMSAPDFWDD NDKAQGIISE
MNAIKSVVEQ YEKLDNERTD LEDMQEILEM EDDDELAAEW TENVKALSGK VDAFELQLLL
SEPYDKANAI LELHPGAGGT ESQDWASMLY RMYTRWAEKR GFKVELLDYL PGDEAGIKSV
TIMVKGYNAY GYLKAEKGVH RLVRISPFDA SGRRHTSFVS CDVVPEIPDD VQIEIRPEDL
RVDTYRSSGA GGQHINKTDS AVRLTHIPTG IVVACQTERS QISNRERAMK MLQSKLYELE
IQKQQEELAA IRGEQKDIAW GSQIRSYVFH PYSMVKDHRT SVETGNVGAV MDGDLDAFID
GYLRSQIKQE VQ
//