ID D1W5G7_9BACT Unreviewed; 374 AA.
AC D1W5G7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=HMPREF0650_1464 {ECO:0000313|EMBL:EFA92227.1};
OS Hoylesella buccalis ATCC 35310.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=679190 {ECO:0000313|EMBL:EFA92227.1, ECO:0000313|Proteomes:UP000005283};
RN [1] {ECO:0000313|EMBL:EFA92227.1, ECO:0000313|Proteomes:UP000005283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35310 {ECO:0000313|EMBL:EFA92227.1,
RC ECO:0000313|Proteomes:UP000005283};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Prevotella buccalis ATCC 35310.";
RL Submitted (DEC-2009) 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:EFA92227.1}.
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DR EMBL; ADEG01000046; EFA92227.1; -; Genomic_DNA.
DR RefSeq; WP_004349006.1; NZ_ADEG01000046.1.
DR AlphaFoldDB; D1W5G7; -.
DR STRING; 679190.HMPREF0650_1464; -.
DR eggNOG; COG1186; Bacteria.
DR Proteomes; UP000005283; 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}.
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 374 AA; 43312 MW; AA92DBA6DE2B2BD4 CRC64;
MITSDQLKDV MERAEALHRY LNIDQKKVEF EEEQLRTQAP DFWEDPKRAQ EQMIKVKGIE
KWLVGYQQVR QLADELELAF DFYRDEMITE DELDADYAKA VAAIEHLEMK NMLRQTEDPM
DCVMKINSGA GGTESQDWAQ MLMRMYMRWA EAHDYKCTIS DIQDGDEAGI KSVTMKIEGG
EYAYGYLKSE NGVHRLVRVS PFNAQGKRMT SFASVFVSPL VDDTIEVFVD PARVSWDTFR
SSGAGGQNVN KVESGVRLRY QYEDPDTGEE EEILIENTET RDQPKNRAKA MQLLKSQLYD
RAMKKRLEAQ AKIEAGKKKI EWGSQIRSYV FDDRRVKDHR TNYQTTDVDA VMDGKLDEFI
KAYLMEFPVA DEND
//
