ID A0A1K1LJ05_9BACT Unreviewed; 373 AA.
AC A0A1K1LJ05;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN02910409_0225 {ECO:0000313|EMBL:SFW10860.1};
OS Prevotellaceae bacterium HUN156.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae.
OX NCBI_TaxID=1520830 {ECO:0000313|EMBL:SFW10860.1, ECO:0000313|Proteomes:UP000182805};
RN [1] {ECO:0000313|EMBL:SFW10860.1, ECO:0000313|Proteomes:UP000182805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HUN156 {ECO:0000313|EMBL:SFW10860.1,
RC ECO:0000313|Proteomes:UP000182805};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FPIT01000003; SFW10860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K1LJ05; -.
DR STRING; 1520830.SAMN02910409_0225; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000182805; 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:UP000182805}.
FT DOMAIN 240..256
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 247
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 373 AA; 43275 MW; 26AA9855A202EB80 CRC64;
MITQDQLKDV LDRADKLKHY LKIDEKKIEF EEEDLRTQAP DFWEDQKRAE EQMKKVKAIK
KWIDGYQEVR TAADELQLAF DFYKEEMVTE EEVDEGYRRA IDAIEALELK NMLRQKEDPM
EAVLKINSGA GGTEAQDWAQ MLMRMYQRWA EAHGYKVSIA NLQDGDEAGI KSVTMQIEGG
EYAYGYLKSE NGVHRLVRVS PYNAQGKRMT SFASVFVSPL VDDTIEVYVD PAKLSWDTFR
SSGAGGQNVN KVESGVRLRY WYTDPDTGEE EEILIENTET RDQPKNKERA MALLRSQLYD
RAMQKRLEAQ AKIEAGKKKI EWGSQIRSYV FDDRRVKDHR TNYQTSDVDG VMDGKIDEFI
KAYLMEFPVN DED
//
