ID A0A1X6YQI6_9RHOB Unreviewed; 373 AA.
AC A0A1X6YQI6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|HAMAP-Rule:MF_00094, ECO:0000256|NCBIfam:TIGR00020};
DE Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094,
GN ECO:0000313|EMBL:SLN27527.1};
GN ORFNames=ROJ8625_01137 {ECO:0000313|EMBL:SLN27527.1};
OS Roseivivax jejudonensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1529041 {ECO:0000313|EMBL:SLN27527.1, ECO:0000313|Proteomes:UP000193570};
RN [1] {ECO:0000313|EMBL:SLN27527.1, ECO:0000313|Proteomes:UP000193570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8625 {ECO:0000313|EMBL:SLN27527.1,
RC ECO:0000313|Proteomes:UP000193570};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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; FWFK01000002; SLN27527.1; -; Genomic_DNA.
DR RefSeq; WP_085790900.1; NZ_FWFK01000002.1.
DR AlphaFoldDB; A0A1X6YQI6; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000193570; 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 FunFam; 3.30.160.20:FF:000004; Peptide chain release factor 1; 1.
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:SF3; CLASS I PEPTIDE CHAIN RELEASE FACTOR; 1.
DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Reference proteome {ECO:0000313|Proteomes:UP000193570}.
FT DOMAIN 242..258
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 249
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 373 AA; 41349 MW; D0BB0DBB7518A00D CRC64;
MRAEAENTVA RIEKSLDLLG QRLDWETAEH RLEEFNARVE DPDLWNDPAA AQKLMRDRQM
LVDQMETYRS IKQDLADQKE LIEMGEAEGD EEIVSEAEGA LKSLAETAAT KELEALLDGE
ADGNDTFLEI NAGAGGTEAC DWAQMLQRMY VRWAESKGYD VELQSEEPGS EAGIKSCAYK
ISGPNAYGWL KTESGVHRLV RISPFGKGTR ETSFASVWVY PVVDDNIEIE VNPADIRVDT
FRSSGAGGQH VNTTDSAVRI THHPTGIVVT SSEKSQHQNR DIAMKALKSR LYQMELDRRH
AEINAQHEAK GEAGWGNQIR SYVLQPYQMV KDLRTSVETS DTSGVLDGAL DPFMAATLAL
KVSGKARADA RED
//
