ID A0A1Y4AHI6_9BACE Unreviewed; 371 AA.
AC A0A1Y4AHI6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=B5F91_04835 {ECO:0000313|EMBL:OUO21875.1};
OS Bacteroides sp. An322.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1965632 {ECO:0000313|EMBL:OUO21875.1, ECO:0000313|Proteomes:UP000195527};
RN [1] {ECO:0000313|Proteomes:UP000195527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An322 {ECO:0000313|Proteomes:UP000195527};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO21875.1}.
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DR EMBL; NFIN01000006; OUO21875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4AHI6; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000195527; 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:UP000195527}.
FT DOMAIN 239..255
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 246
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 371 AA; 42579 MW; 948C21A53A7E20FE CRC64;
MITTDQLKDI KERTEALYRY LDIENKTVQV EEEQLRTQAP GFWDDAKKAE AQMKKVKTLQ
GWIDGYREVK TLADELELAF DFYKDELVSE AEVDEAYAKA LKAVEELELK NMLRSEADQM
DCVLKINSGA GGTESQDWAS MLMRMYMRWA ESHGYKLSVA NLQEGDEAGI KTVTMNLEGA
YAYGYLKGEN GVHRLVRVSP YNAQGKRMTS FASVFVTPLV DDSIEVTVEP ARLSWDTFRS
GGAGGQNVNK VESGVRLRYQ YKDPYTGEEE EILIENTETR DQPKNKENAM RQLRSILYDK
ELQHRMEEQA KVEAGKKKIE WGSQIRSYVF DDRRVKDHRT NFQTSDVNGV MDGKIDGFIK
AYLMEFSDSE M
//
