ID A0A1H9KSB6_9SPHN Unreviewed; 375 AA.
AC A0A1H9KSB6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN05518866_104135 {ECO:0000313|EMBL:SER02022.1};
OS Sphingobium sp. YR768.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1884365 {ECO:0000313|EMBL:SER02022.1, ECO:0000313|Proteomes:UP000199142};
RN [1] {ECO:0000313|Proteomes:UP000199142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR768 {ECO:0000313|Proteomes:UP000199142};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FOGE01000004; SER02022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9KSB6; -.
DR STRING; 1884365.SAMN05518866_104135; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000199142; 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:UP000199142}.
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; 41788 MW; DE192C6D198AFABE CRC64;
MRAEAQQYID RIDAALDLLR RFLDWDRALR RLDELNARVE DPTLWDNAKL AQEVMRERTR
LDSAIGATRS IEGEKTDNAE LIDMADAEGD EDMVSEAIAA LKALAERADE DKIKALLAGE
ADASDTYLEI HAGAGGTESQ DWAEILSRMY RRWAERRGYK VDLVDYQAGE TAGIKSATFL
IKGENAYGYA KTESGVHRLV RISPYDSAAR RHTSFSSVWV YPVIDDNIDI EIKESDLKID
TYRASGAGGQ HVNTTDSAVR ITHVPSGIIV ASQNDRSQHK NRATAMNMLK ARLYEAELRK
REEAANTDYQ AKTEIGWGHQ IRSYVLQPYQ LVKDLRTGVT STSPDDVLDG ALDPFMAAAL
SQKVTGESVD VEDVD
//
