ID A0A1C7GN68_9FIRM Unreviewed; 375 AA.
AC A0A1C7GN68;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=A4V00_06985 {ECO:0000313|EMBL:ANU53794.1};
OS Hungateiclostridiaceae bacterium KB18.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1834198 {ECO:0000313|EMBL:ANU53794.1, ECO:0000313|Proteomes:UP000092525};
RN [1] {ECO:0000313|Proteomes:UP000092525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KB18 {ECO:0000313|Proteomes:UP000092525};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-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; CP015400; ANU53794.1; -; Genomic_DNA.
DR RefSeq; WP_066536348.1; NZ_CP021422.1.
DR AlphaFoldDB; A0A1C7GN68; -.
DR STRING; 1834198.A4V00_06985; -.
DR GeneID; 83334238; -.
DR KEGG; ruk:A4V00_06985; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000092525; Chromosome.
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.
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:UP000092525}.
FT DOMAIN 85..195
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT MOD_RES 252
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 375 AA; 41661 MW; 603BF8D9D505E3E6 CRC64;
MLQFEELSRQ LSGQRQALTE LGDSLGLERL REEVEMLELK SAEPGFWDDM ANAQKVTQRM
AGLKAKDESY QKLCSRCEDA AALIELGDEA EDLSLIEEIQ AEIDGVAGEI ANMKLSTLLT
GEYDGHNAIL TFHAGSGGTE AQDWAEMLFR MYGRWAERRG FKVTTLDYLD GDEAGLKSAS
ILVEGENAYG YLKSEAGVHR LVRVSPFDAA GRRHTSFSSL EVMPEIEEDN SVEISPDDIK
MEVYRASGAG GQKVNKTSSA VRLIHIPTGI VVSCQVERSQ YQNRDVAMKM LISKLVEIKE
RENLEKISDI KGEQKEITWG SQIRSYVFMP YTMVKDHRTG FETGNVNGVM DGDLDGFINA
YLTAKSQGTL GENIE
//
