ID A0A197ST43_9ACTN Unreviewed; 368 AA.
AC A0A197ST43;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=A8W25_11255 {ECO:0000313|EMBL:OAR26052.1};
OS Streptomyces sp. ERV7.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1322334 {ECO:0000313|EMBL:OAR26052.1, ECO:0000313|Proteomes:UP000078470};
RN [1] {ECO:0000313|EMBL:OAR26052.1, ECO:0000313|Proteomes:UP000078470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERV7 {ECO:0000313|EMBL:OAR26052.1,
RC ECO:0000313|Proteomes:UP000078470};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-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:OAR26052.1}.
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DR EMBL; LYOY01000029; OAR26052.1; -; Genomic_DNA.
DR RefSeq; WP_067159681.1; NZ_LYOY01000029.1.
DR AlphaFoldDB; A0A197ST43; -.
DR STRING; 1322334.A8W25_11255; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000078470; 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:UP000078470}.
FT DOMAIN 244..260
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 52..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 368 AA; 40955 MW; 5EACFF7C6F66C922 CRC64;
MAVVDVSEEL KSLSSTMGSI EAVLDLDKLR ADIAVLEEQA AAPSLWDDPE AAQKITSKLS
HLQAEVRKTE ALRGRIDDLS VLFELAEEMD DADTLAEAEA ELVSVRKALD EMEVRTLLSG
EYDEREALVN IRAEAGGVDA SDFAERLQRM YLRWAERHGY STEVYETSYA EEAGIKSTTF
VVKAPYAYGT LSVEQGTHRL VRISPFDNQG RRQTSFAGVE ILPVVESSDH VEIDESELRV
DVYRASGPGG QGVNTTDSAV RITHLPTGIV VSCQNERSQI QNKASAMNVL QAKLLERQRQ
EERARMDALK GDGGSSWGNQ MRSYVLHPYQ MVKDLRTEFE VGNPQSVLDG EIDGFLEAGI
RWRKQQEK
//
