ID A0A317EK25_9PROT Unreviewed; 375 AA.
AC A0A317EK25;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, 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 ORFNames=DKG74_02105 {ECO:0000313|EMBL:PWR25773.1};
OS Zavarzinia aquatilis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodospirillales; Zavarziniaceae; Zavarzinia.
OX NCBI_TaxID=2211142 {ECO:0000313|EMBL:PWR25773.1, ECO:0000313|Proteomes:UP000245461};
RN [1] {ECO:0000313|EMBL:PWR25773.1, ECO:0000313|Proteomes:UP000245461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-AS {ECO:0000313|EMBL:PWR25773.1,
RC ECO:0000313|Proteomes:UP000245461};
RA Lee Y., Jeon C.O.;
RT "Zavarzinia sp. HR-AS.";
RL Submitted (MAY-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:PWR25773.1}.
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DR EMBL; QGLE01000001; PWR25773.1; -; Genomic_DNA.
DR RefSeq; WP_109902090.1; NZ_QGLE01000001.1.
DR AlphaFoldDB; A0A317EK25; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000245461; 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 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Reference proteome {ECO:0000313|Proteomes:UP000245461}.
FT DOMAIN 243..259
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 54..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; 41839 MW; AD79151CBA6D39E6 CRC64;
MRADVESLNA EIKQSLELLR RHLDWDVANV RLEELNARVE DPSLWNDPAE AQKIMRERTR
LDDAIGAYKR LEAELRDMLE LAEMAEVEGD ESMIDDAVAN LRRVRDEAGE AEVKALLSGE
ADGNDTYLEV NAGAGGTEAQ DWAEMMLRMY TRWAERKGYK VELIEDSPGE QAGLKSATIL
VKGLNAYGWM KTESGVHRLV RISPFDSNAR RQTSFASVWV YPVVDDAIEI EILDKDLRVD
TYRASGAGGQ HVNKTDSAIR ITHIPTGIVV ACQADRSQHK NRSQAMSMLK ARLYERELQI
REEAAKATEE TKTAIGWGHQ IRSYVLQPYQ MVKDLRTGAE TSDTQGVLNG DIDRFMAAAL
AARVEGGGAE VSDLD
//
