ID A0A133ZMN4_9CORY Unreviewed; 367 AA.
AC A0A133ZMN4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=HMPREF0307_00101 {ECO:0000313|EMBL:KXB56682.1};
OS Corynebacterium sp. DNF00584.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1384076 {ECO:0000313|EMBL:KXB56682.1, ECO:0000313|Proteomes:UP000070591};
RN [1] {ECO:0000313|EMBL:KXB56682.1, ECO:0000313|Proteomes:UP000070591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00584 {ECO:0000313|EMBL:KXB56682.1,
RC ECO:0000313|Proteomes:UP000070591};
RA Oliw E.H.;
RL Submitted (JAN-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|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:KXB56682.1}.
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DR EMBL; LSCZ01000002; KXB56682.1; -; Genomic_DNA.
DR RefSeq; WP_066484784.1; NZ_KQ959727.1.
DR AlphaFoldDB; A0A133ZMN4; -.
DR GeneID; 79852298; -.
DR PATRIC; fig|1384076.3.peg.97; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000070591; 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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094};
KW Reference proteome {ECO:0000313|Proteomes:UP000070591}.
FT DOMAIN 240..256
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 84..111
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 247
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 367 AA; 40623 MW; 8BB089FA7171F71B CRC64;
MRPETSATID QLSATLTSIE KVMDPETLRE TVRELEATAG DPSLWDDPAH AQQVTTKLSA
AQAKLRRLGE LRGRLDDLPV MYELAEEEGD ASVADEELAS LQAAIESLEV TTMLSGDYDD
REAVINIRSG AGGVDAADWA EMLMRMYTRW ADKHGHKVDV YDISYAEEAG IKSATFVVHG
EYMYGQLSVE QGTHRLVRIS PFDSQARRQT SFAEVEVLPV VEQTDHIDVP DSDLRVDVYR
SSGPGGQSVN TTDSAVRLTH LPTGIVVTCQ NEKSQIQNKA SALRVLQAKL LERKRQEERA
AMDALGAGGN ASWGNQMRNY VLHPYQMVKD LRTNYEVGDP QKVLDGDIDG FLEAAIRWRM
AAERAAE
//
