ID A0A238KL09_9RHOB Unreviewed; 375 AA.
AC A0A238KL09;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:SMX42772.1};
GN ORFNames=COL8621_02068 {ECO:0000313|EMBL:SMX42772.1};
OS Actibacterium lipolyticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1524263 {ECO:0000313|EMBL:SMX42772.1, ECO:0000313|Proteomes:UP000202922};
RN [1] {ECO:0000313|Proteomes:UP000202922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8621 {ECO:0000313|Proteomes:UP000202922};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAY-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; FXYE01000002; SMX42772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238KL09; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000202922; 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 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:UP000202922}.
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; 41530 MW; 7FBF58ADA951638A CRC64;
MRADTQNTVE EIRKSLALLA QRLDWETAEH RLEEFNARVE DPDLWNDAAN AQKLMRERQA
LVDSIDVYKG IEQELSDNIE LIELGEMEDD AEVVSEAETA LKALAEKAAK KEIEALLNGE
ADANDTFLEI NSGAGGTESC DWASMLARMY VRWAEKKGYK VELQSESAGE EAGIKSASYK
ISGHNAYGWL KSESGVHRLV RISPYDSAAR RHTSFSSVWV YPVVDDNIEI EVNPADIRVD
TYRSSGAGGQ HVNTTDSAVR ITHAPTGIVV TSSEKSQHQN RDIAMKALKS RLYQMELEKR
TASIQEAHEA KGDAGWGNQI RSYVLQPYQM VKDLRTNVET SDTQGVLDGD LDQFMAATLA
MDVAGKSRGE AQAEA
//
