ID A0A2U3A0N4_9ACTN Unreviewed; 367 AA.
AC A0A2U3A0N4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-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 ECO:0000313|EMBL:PWI18050.1};
GN ORFNames=DI272_30795 {ECO:0000313|EMBL:PWI18050.1};
OS Streptomyces sp. Act143.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI18050.1, ECO:0000313|Proteomes:UP000245455};
RN [1] {ECO:0000313|EMBL:PWI18050.1, ECO:0000313|Proteomes:UP000245455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Act143 {ECO:0000313|EMBL:PWI18050.1,
RC ECO:0000313|Proteomes:UP000245455};
RA Valanrebinro G., Kumari S., Rameshkumar N.;
RT "Actinomycin D producing novel Streptomyces isolated from the rhizosphere
RT of saline tolerant kaipad rice and its draft genome analysis.";
RL Submitted (MAY-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:PWI18050.1}.
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DR EMBL; QFRX01000001; PWI18050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3A0N4; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000245455; 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:UP000245455}.
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 367 AA; 41005 MW; D48AFCFB98C8A9DB CRC64;
MAVVDVSEEL KSLSSTMESI EAVLDLDKLR ADIAVLEEQA AAPSLWDNPD EAQKITSKLS
HLQAEVRKAE ALRGRIDDLA VLFEMAEEED DPDTRAEAES ELASVKKALD EMEVRTLLSG
EYDAREALVN IRAEAGGVDA ADFAEQLQRM YLRWAERHGY KTEVYETSYA EEAGIKSTTF
AVQVPYAYGQ LSVEQGTHRL VRISPFDNQG RRQTSFAGVE VLPVVEQTDH IDIDESDLRI
DVYRSSGPGG QGVNTTDSAV RITHLPTGIV VSCQNERSQI QNKATAMNVL QAKLLERQRQ
EERAKMDALK DGGSSWGNQM RSYVLHPYQM VKDLRTEFEV GNPQAVLDGE IDGFLEAGIR
WRKQQEK
//
