ID V5AFG8_9PROT Unreviewed; 345 AA.
AC V5AFG8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 ECO:0000313|EMBL:ESS14390.1};
GN ORFNames=MOLA814_02024 {ECO:0000313|EMBL:ESS14390.1};
OS Betaproteobacteria bacterium MOLA814.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1408164 {ECO:0000313|EMBL:ESS14390.1, ECO:0000313|Proteomes:UP000017838};
RN [1] {ECO:0000313|EMBL:ESS14390.1, ECO:0000313|Proteomes:UP000017838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOLA814 {ECO:0000313|EMBL:ESS14390.1,
RC ECO:0000313|Proteomes:UP000017838};
RX PubMed=24356832;
RA Courties A., Riedel T., Jarek M., Intertaglia L., Lebaron P., Suzuki M.T.;
RT "Genome Sequence of Strain MOLA814, a Proteorhodopsin-Containing
RT Representative of the Betaproteobacteria Common in the Ocean.";
RL Genome Announc. 1:e01062-13(2013).
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}.
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:ESS14390.1}.
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DR EMBL; AYMW01000002; ESS14390.1; -; Genomic_DNA.
DR AlphaFoldDB; V5AFG8; -.
DR STRING; 1408164.MOLA814_02024; -.
DR PATRIC; fig|1408164.3.peg.2131; -.
DR eggNOG; COG1186; Bacteria.
DR Proteomes; UP000017838; 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 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:UP000017838}.
FT DOMAIN 225..241
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 232
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 345 AA; 38424 MW; 0168DB08F2DA54B0 CRC64;
MSYGGIFDVD SKAARLSEVE AALEDPSVWN DPKRAQDLGR EKKSLDDVVG VLFKLGTDLT
DNAELFEMSQ DDHAGLLMIQ DDAEALLGVV ERLEFRRMFN QPADPSNCFI DIQSGAGGTE
ACDWASILMR QYLRYAERQG FKTTIEDETP GDIAGIKGTT IRVDGEYAFG LLRTESGVHR
LVRKSPFDSA GGRHTSFASV FVYPEVDDSI EIDINPSDVR TDTYRASGAG GQHINKTDSA
VRLTHIPTGT VVQCQDGRSQ HGNRDVAWKR LRSKLYDLEM RKRQDEQQKL EDGKTDVGWG
HQIRSYVLDQ SRIKDLRTGV EATNTQKVLD GDLDMFIQAS LKQGV
//
