ID A0A923HD90_9FLAO Unreviewed; 369 AA.
AC A0A923HD90;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
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:MBC3759026.1};
GN ORFNames=H7U19_11455 {ECO:0000313|EMBL:MBC3759026.1};
OS Hyunsoonleella aquatilis.
OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2762758 {ECO:0000313|EMBL:MBC3759026.1, ECO:0000313|Proteomes:UP000656244};
RN [1] {ECO:0000313|EMBL:MBC3759026.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SJ7 {ECO:0000313|EMBL:MBC3759026.1};
RA Kim I.;
RT "Hyunsoonleella sp. strain SJ7 genome sequencing and assembly.";
RL Submitted (AUG-2020) 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:MBC3759026.1}.
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DR EMBL; JACNMF010000003; MBC3759026.1; -; Genomic_DNA.
DR RefSeq; WP_186562451.1; NZ_JACNMF010000003.1.
DR AlphaFoldDB; A0A923HD90; -.
DR Proteomes; UP000656244; 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:000040; 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|ARBA:ARBA00022490, 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:UP000656244}.
FT DOMAIN 239..255
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 246
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 369 AA; 42321 MW; 732F2FF9B92ADD26 CRC64;
MITSDQIKDL NTRLDKLRHY LDIDAKLIEI QNEEEQTFDP NFWNDPKSAE AVMKSLRVKK
KWVQDYKDVK TLIEDLEVIY EFFKEGESTQ EDVENRYSKA SNLLEDIEFR NMLSEEGDSL
SAVLQITAGA GGTESCDWAS MLMRMYLMYA EKNSFKMKEL NFQEGDVAGI KTVTLEIEGD
FAFGWLKGEN GVHRLVRISP FDSNAKRHTS FASVYVYPLV DDTIEIEINP ADIEITTARS
SGAGGQNVNK VETKVQLTHK PTGIQISCSE TRSQHDNRTR AMQMLKSQLY EIELQKQLSQ
RDDIEASKMK IEWGSQIRNY VMHPYKLVKD VRTNHETGNV DAVMNGDIDA FLKAYLMMMG
QKEEDTSQL
//
