ID A0A1D9NZH1_9FIRM Unreviewed; 380 AA.
AC A0A1D9NZH1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
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=bhn_I0577 {ECO:0000313|EMBL:AOZ95611.1};
OS Butyrivibrio hungatei.
OC Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC Lachnospiraceae; Butyrivibrio.
OX NCBI_TaxID=185008 {ECO:0000313|EMBL:AOZ95611.1, ECO:0000313|Proteomes:UP000179284};
RN [1] {ECO:0000313|Proteomes:UP000179284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB2003 {ECO:0000313|Proteomes:UP000179284};
RA Palevich N., Kelly W.J., Leahy S.C., Altermann E., Rakonjac J.,
RA Attwood G.T.;
RT "The complete genome sequence of the rumen bacterium Butyrivibrio hungatei
RT MB2003.";
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; CP017831; AOZ95611.1; -; Genomic_DNA.
DR RefSeq; WP_071175375.1; NZ_CP017831.1.
DR AlphaFoldDB; A0A1D9NZH1; -.
DR KEGG; bhu:bhn_I0577; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000179284; Chromosome I.
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:000010; 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|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:UP000179284}.
FT DOMAIN 247..263
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 254
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 380 AA; 42628 MW; 601A21E3A8719A00 CRC64;
MVVLDQMKVE IQNLQDTLKE VTASLDLNTK KKIIEELSRE MEEPGFWDDA EKANKKTKDL
KNMQDLVEGI EKLNTQYGDI IDLIDMQNAE GVDDEDMAAE IRAELDDFET TLENIRISNL
LNQPYDKYDV ILRLNAGAGG TEACDWASML YRMYTRWAER KGFTTEVLDL LDGDEAGIKS
VTFQISGTNA YGLLKSEHGV HRLVRISPFN AQAKRQTSFV SCDVMPDIEE DVDVEINPDD
LRIDTYRSSG AGGQHINKTS SAVRITHIPT GVVVACQNER SQFQNKDKAM QMLKAKLFIM
KQEEQAAKLA GIRGEVMDNA WGSQIRSYVL QPYTMVNDTR TGFKASNADA VLDGDLDQFI
NAYLKWLATG GKPVGDTSEE
//
