ID A0A2V4MX32_9ACTN Unreviewed; 369 AA.
AC A0A2V4MX32;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=C7C46_31365 {ECO:0000313|EMBL:PYC66485.1};
OS Streptomyces tateyamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=565073 {ECO:0000313|EMBL:PYC66485.1, ECO:0000313|Proteomes:UP000248039};
RN [1] {ECO:0000313|EMBL:PYC66485.1, ECO:0000313|Proteomes:UP000248039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21389 {ECO:0000313|EMBL:PYC66485.1,
RC ECO:0000313|Proteomes:UP000248039};
RA Schwalen C.J., Hudson G.A., Mitchell D.A.;
RT "Bioinformatic expansion and discovery of thiopeptide antibiotics.";
RL Submitted (MAR-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|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:PYC66485.1}.
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DR EMBL; PYBW01000174; PYC66485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4MX32; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000248039; 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:UP000248039}.
FT DOMAIN 244..260
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 369 AA; 41233 MW; 808DBB3DACAA3A55 CRC64;
MAAVDPSEEL KNLETTMGSI EAVLDLEKIR ADISRLEEEA AAPNLWDDVA SAQKVTSRLS
FLQAELRRVL NLRSRIDDVR VLFELAEEMA DADTRVEAEA ELSATKKVVE ELEVRTLLSG
EYDAREALVN IRAEAGGVDA ADFAEQLMRM YLRWAERHGY PTEVYDTSYA EEAGIKSATF
TVKSPYAYGT LSVEQGTHRL VRISPFDNQG RRQTSFAGVE VLPVVEQSDH VTIDEGELRV
DVYRASGPGG QGVNTTDSAV RITHLPTGIV VSCQNERSQI QNKASAMNVL QSKLLERRRQ
EEKAMMDALK DGGSSWGNQM RSYVLHPYQM VKDLRTEYEV GNPQSVLDGD IDGFIEAGIR
WRKQRETAE
//
