ID A0A1I1DPG9_9FIRM Unreviewed; 380 AA.
AC A0A1I1DPG9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|ARBA:ARBA00019192, 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=SAMN02910398_00702 {ECO:0000313|EMBL:SFB76717.1};
OS Butyrivibrio sp. YAB3001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520812 {ECO:0000313|EMBL:SFB76717.1, ECO:0000313|Proteomes:UP000198944};
RN [1] {ECO:0000313|EMBL:SFB76717.1, ECO:0000313|Proteomes:UP000198944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YAB3001 {ECO:0000313|EMBL:SFB76717.1,
RC ECO:0000313|Proteomes:UP000198944};
RA de Groot N.N.;
RL Submitted (OCT-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|ARBA:ARBA00002613, 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; FOKR01000002; SFB76717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1DPG9; -.
DR STRING; 1520812.SAMN02910398_00702; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000198944; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000198944}.
FT DOMAIN 247..263
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 4..118
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 254
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 380 AA; 42721 MW; 27D80ADA5EAD7DA3 CRC64;
MVILDQMKVE IQNLQETLKE VTASLDLNTK KKIIEELSRE MEEPGFWDNA EKANKKTKDL
KNMQDLVANI ERLNNQYTDI IDLIDMQNAE GVDDDDMAAE IRAELDDFED TLENIRISNL
LNGPYDKYDV ILRLNAGAGG TEACDWASML YRMYTRWAER KGFTTEVLDL LDGDEAGIKS
VTFQISGTNA YGLLKSEHGV HRLVRISPFN AQAKRQTSFV SCDVMPDIEE DVDIDINPDD
LRIDTYRSSG AGGQHINKTS SAVRITHIPT GVVVACQNER SQFQNKDKAM QMLKAKLFIM
KQEENQAKLD GIRGEVKDNA WGSQIRSYVL QPYTMVNDTR TGFKASNADG VLDGELDPFI
NAYLKWLATG GKPVGDTSEE
//
