ID A0A2S5JJP6_9RHOB Unreviewed; 375 AA.
AC A0A2S5JJP6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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 ORFNames=LV82_00949 {ECO:0000313|EMBL:PPB81737.1};
OS Albidovulum inexpectatum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albidovulum.
OX NCBI_TaxID=196587 {ECO:0000313|EMBL:PPB81737.1, ECO:0000313|Proteomes:UP000239736};
RN [1] {ECO:0000313|EMBL:PPB81737.1, ECO:0000313|Proteomes:UP000239736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12048 {ECO:0000313|EMBL:PPB81737.1,
RC ECO:0000313|Proteomes:UP000239736};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JAN-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:PPB81737.1}.
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DR EMBL; PRDS01000002; PPB81737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5JJP6; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000239736; 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:UP000239736}.
FT DOMAIN 243..259
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 87..114
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 250
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 375 AA; 41931 MW; 9B62BD0AFB319548 CRC64;
MRAEIENIVD SIRKSLNLLG QRMDLETAEH RLEEMNAMIE DGDLWSDPER AQKLMRDRQM
LLDQIETYRR IERDLNDNVE LIEMGEAEGD SEVVEEAENA LRELKTLAEQ KELEALLDGE
ADSNDTFLEI NAGAGGTESC DWAAMLARMY VRWAEKKGYK VELMSESPGE EAGIRSATYR
ISGPNAYGWL KSESGVHRLV RISPFDSSAR RHTSFCSVWV YPVVDDNIEI VIPDSDIRID
TFRSSGAGGQ HVNTTDSAVR ITHIPTGIVV TSSEKSQHQN RANAMAALKA RLYQLELDKR
NAEIAAQHEA KGEAAWGNQI RSYVLHPYQM VKDLRTGHET SDTQGVLDGD LDAFMAATLA
MKVAGKSRAE AQTQD
//
