ID A0A3A9GIA0_9FIRM Unreviewed; 377 AA.
AC A0A3A9GIA0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ECO:0000313|EMBL:RKJ64173.1};
GN ORFNames=D7Y06_12840 {ECO:0000313|EMBL:RKJ64173.1};
OS Roseburia sp. 1XD42-69.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=2320088 {ECO:0000313|EMBL:RKJ64173.1, ECO:0000313|Proteomes:UP000279120};
RN [1] {ECO:0000313|EMBL:RKJ64173.1, ECO:0000313|Proteomes:UP000279120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1XD42-69 {ECO:0000313|EMBL:RKJ64173.1,
RC ECO:0000313|Proteomes:UP000279120};
RA Liu C.;
RT "Murine metabolic-syndrome-specific gut microbial biobank.";
RL Submitted (SEP-2018) 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}.
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:RKJ64173.1}.
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DR EMBL; RAZG01000024; RKJ64173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9GIA0; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000279120; 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:UP000279120}.
FT DOMAIN 245..261
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 50..90
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 252
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 377 AA; 42341 MW; 5FBE4C1B48AB6ECF CRC64;
MVELDQFKTT LNTYKKPLLE VRDSLDLAGK KQKIQELERE MEAPDFWDNV ETSQAKMKEL
KSLKDDVETL AKLTGQFEDI ETLIEMADEE NDASLIPEVE SELKGFIETF ESIRMKTLLS
GEYDRDNAIV SLHAGAGGTE SCDWAAMLYR MFTRFAGDKG FSVEVLDSLD GEEAGIKSIT
FQVNGENAYG YLKSEKGVHR LVRISPFNAA GKRQTSFVSC DVMPDIEEDL DVEINEEDIR
IDTYRSSGAG GQHINKTSSA IRITHFPTGI VVQCQNERSQ HMNKDKAMQM LKAKLFLLKQ
QENAQKAACI RGEVTDIGWG NQIRSYVMQP YTMVKDHRTG AETGNVGSVL DGNLDIFING
YLKWLSLGCP KRADSEE
//
