ID A0A1M4T447_LOKAT Unreviewed; 375 AA.
AC A0A1M4T447;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 28.
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 ORFNames=SAMN05444339_101245 {ECO:0000313|EMBL:SHE39108.1};
OS Loktanella atrilutea.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Loktanella.
OX NCBI_TaxID=366533 {ECO:0000313|EMBL:SHE39108.1, ECO:0000313|Proteomes:UP000183987};
RN [1] {ECO:0000313|Proteomes:UP000183987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29326 {ECO:0000313|Proteomes:UP000183987};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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}.
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DR EMBL; FQUE01000001; SHE39108.1; -; Genomic_DNA.
DR RefSeq; WP_072855377.1; NZ_FQUE01000001.1.
DR AlphaFoldDB; A0A1M4T447; -.
DR STRING; 366533.SAMN05444339_101245; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000183987; 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:000010; Peptide chain release factor 2; 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:UP000183987}.
FT DOMAIN 243..259
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 250
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 375 AA; 41750 MW; 522BCDFD4F21C87E CRC64;
MRAETQNTIE AIEKSLSLLA QRLDYDTAPH RLEEFNARVE DPTLWDDPTH AQKLMRERQM
LVDAVESYEG IRQELADNVE LIEMGEMEDD AEIVSDAEEA LTALKARAAE KELEALLNGE
ADGNDTFLEI NAGAGGTESC DWANMLARMY VRWAEKKGYK VELQSESAGE EVGIKSAAYK
ITGPNAYGWL KSESGVHRLV RISPYDSAAK RHTSFSSVWV YPVVDDNIEI DVQPNDIRID
TYRSSGAGGQ HVNTTDSAVR ITHHPTGIVV TSSEKSQHQN RDIAMKALKS RLYQMELDKR
NAAINEAHDN KGDAGWGNQI RSYVLQPYQM VKDLRTRHET SDTQGVLDGD LDAFMAATLA
MDVSGKSRAE ANLDD
//
