ID A0A0D7KDE7_9BURK Unreviewed; 300 AA.
AC A0A0D7KDE7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=RP29_02255 {ECO:0000313|EMBL:KJA12074.1};
OS Acidovorax temperans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA12074.1, ECO:0000313|Proteomes:UP000032566};
RN [1] {ECO:0000313|EMBL:KJA12074.1, ECO:0000313|Proteomes:UP000032566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY4 {ECO:0000313|EMBL:KJA12074.1,
RC ECO:0000313|Proteomes:UP000032566};
RA Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.;
RT "Isolation of bacteria from lake water.";
RL Submitted (DEC-2014) 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:KJA12074.1}.
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; JXYQ01000007; KJA12074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7KDE7; -.
DR STRING; 80878.RP29_02255; -.
DR PATRIC; fig|80878.5.peg.3515; -.
DR Proteomes; UP000032566; 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:UP000032566}.
FT DOMAIN 180..196
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 187
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 300 AA; 33742 MW; E3F071C27990C874 CRC64;
MVVTLDKLTR ELADNAELYE MSKEEGDEAG LLTIEAEADK LRPLIEELEF RRMFSNEADP
LNCFVDIQAG AGGTEACDWA SMLLRQYLKY AERKGFKATV EEETAGDVAG IKSATIKIEG
EYAYGLLRTE TGVHRLVRKS PFDSSGGRHT SFASLFVYPE IDDSIEININ PADVRTDTYR
ASGAGGQHIN KTDSAVRLTH IPTGIVVQCQ DGRSQHSNRD VAWQRLRSRL YDYEMRKRQE
EQQKLEDTKT DVGWGHQIRS YVLDNSRIKD LRTNVEVSAT QKVLDGDLDV FIEASLKQGV
//
