ID A0A0F6TRG1_9GAMM Unreviewed; 349 AA.
AC A0A0F6TRG1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=TQ33_1647 {ECO:0000313|EMBL:AKE52590.1};
OS Kangiella geojedonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC Kangiella.
OX NCBI_TaxID=914150 {ECO:0000313|EMBL:AKE52590.1, ECO:0000313|Proteomes:UP000034071};
RN [1] {ECO:0000313|EMBL:AKE52590.1, ECO:0000313|Proteomes:UP000034071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCS-5 {ECO:0000313|EMBL:AKE52590.1,
RC ECO:0000313|Proteomes:UP000034071};
RA Kim K.M.;
RT "Complete genome sequence of Kangiella geojedonensis strain YCS-5T.";
RL Submitted (FEB-2015) 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; CP010975; AKE52590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F6TRG1; -.
DR STRING; 914150.TQ33_1647; -.
DR KEGG; kge:TQ33_1647; -.
DR PATRIC; fig|914150.5.peg.1668; -.
DR HOGENOM; CLU_036856_6_0_6; -.
DR Proteomes; UP000034071; Chromosome.
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:UP000034071}.
FT DOMAIN 229..245
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 236
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 349 AA; 39285 MW; 11E329F6823A3FF8 CRC64;
MLKRLGGIFD FDAKQERLEE VTKELEQPDV WNDQERAQAL GQERAKLEAV VNTILELEQG
VTDHSDLLEI AVEENDADSA EMIEVEVEGL EKMLAKLEFR RMFSGEMDEN NAYLDIQAGS
GGTEAQDWAS MLLRMYLRWA ESRGFKVEVT EESDGDVAGI KSATIKVDGE YAYGWLRTET
GVHRLVRKSP FDSGNRRHTS FASVFVYPEV DDDIDIEVNP ADLRVDTYRA SGAGGQHVNK
TDSAIRLTHI PTGIVVQCQN DRSQHKNRAE AMKMMKAKLY ELEMQKQREE QQALEDSKSD
IGWGSQIRSY VLDQSRIKDL RTGHESSSTQ AVLDGDLDSF IEASLKAGV
//
