ID A0A5C8KXU9_9GAMM Unreviewed; 374 AA.
AC A0A5C8KXU9;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
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:TXK64423.1};
GN ORFNames=FU658_05895 {ECO:0000313|EMBL:TXK64423.1};
OS Alkalisalibacterium limincola.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Lysobacterales; Lysobacteraceae; Alkalisalibacterium.
OX NCBI_TaxID=2699169 {ECO:0000313|EMBL:TXK64423.1, ECO:0000313|Proteomes:UP000321248};
RN [1] {ECO:0000313|EMBL:TXK64423.1, ECO:0000313|Proteomes:UP000321248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alg18-2.2 {ECO:0000313|EMBL:TXK64423.1,
RC ECO:0000313|Proteomes:UP000321248};
RA Karlyshev A.V.;
RL Submitted (AUG-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}.
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:TXK64423.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VRTS01000003; TXK64423.1; -; Genomic_DNA.
DR RefSeq; WP_147891235.1; NZ_VRTS01000003.1.
DR AlphaFoldDB; A0A5C8KXU9; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000321248; 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:000010; Peptide chain release factor 2; 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|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:UP000321248}.
FT DOMAIN 245..261
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 252
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 374 AA; 41640 MW; 7EA3CFD4CC547794 CRC64;
MIELNPVRQR IADLQGRLDA LRGYLDLDAK AERLEEVNRE LELPDVWNDP ERAQALGRER
SALEKNVNGI RQLDEGLAGA LELIELAESE ADEETAQAVI DDVEGFERDV GKLEFQRMFS
GDLDGANAFI DIQAGAGGTE AQDWAEMLLR MYLRWCESRG WKTELMEASG GDVAGIKSAT
IRVEGDFAYG WIKTETGVHR LVRKSPFDSD NRRHTSFTSV FVSPEVDDKI DIEINPADLK
TDVYRASGAG GQHVNKTESA VRITHVPTGT VVACQNGRSQ HQNRDTAMKM LAARLYELEM
QKRNAEKDAL EATKSDIGWG SQIRNYVLDQ SRIKDLRTGV ERSDTQKVLD GDIDEFVEAA
LKSGLDVGSK RIDA
//
