ID A0A285QR24_9ACTN Unreviewed; 370 AA.
AC A0A285QR24;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN06272789_4087 {ECO:0000313|EMBL:SOB83869.1};
OS Streptomyces sp. 1331.2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938835 {ECO:0000313|EMBL:SOB83869.1, ECO:0000313|Proteomes:UP000219030};
RN [1] {ECO:0000313|Proteomes:UP000219030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1331.2 {ECO:0000313|Proteomes:UP000219030};
RA Varghese N., Submissions S.;
RL Submitted (JUL-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}.
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DR EMBL; OBMJ01000001; SOB83869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285QR24; -.
DR Proteomes; UP000219030; 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:UP000219030}.
FT DOMAIN 244..260
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 88..115
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 370 AA; 40910 MW; 8B0EF8CA6545F657 CRC64;
MAAVDPSEEL KNLDTTMGSI EAVLDLDKIR ADIAVLEEEA AAPNLWDDVA NAQKVTSRLS
FLQGELRRVE GLRSRIDDLG VLFELAEAED DADTRAEAEA ELVSLQKAVE ELEVRTLLSG
EYDAREALIN IRAEAGGVDA ADFAEQLMRM YLRWAERHGY PTEVYDTSYA EEAGIKSATF
TVKAPYAYGT LSVEQGTHRL VRISPFDNQG RRQTSFAGVE VLPVVEQSDH VDIDEGDLRV
DVYRASGPGG QGVNTTDSAV RITHLPTGIV VSCQNERSQI QNKASAMNVL QAKLLERRRQ
EEKAAMDALK DSGSSWGNQM RSYVLHPYQM VKDVRTAYEA GNPQAVLDGD IDGFIEAGIR
WRKQRETSAE
//
