ID A0A2S7U033_9BACT Unreviewed; 355 AA.
AC A0A2S7U033;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=BSZ32_05115 {ECO:0000313|EMBL:PQJ27940.1};
OS Rubritalea profundi.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Rubritaleaceae; Rubritalea.
OX NCBI_TaxID=1658618 {ECO:0000313|EMBL:PQJ27940.1, ECO:0000313|Proteomes:UP000239907};
RN [1] {ECO:0000313|EMBL:PQJ27940.1, ECO:0000313|Proteomes:UP000239907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAORIC-165 {ECO:0000313|EMBL:PQJ27940.1,
RC ECO:0000313|Proteomes:UP000239907};
RA Song J., Yoshizawa S., Kogure K.;
RT "Study of bacterial adaptation to deep sea.";
RL Submitted (DEC-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}.
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:PQJ27940.1}.
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DR EMBL; MQWA01000001; PQJ27940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7U033; -.
DR Proteomes; UP000239907; 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:UP000239907}.
FT DOMAIN 227..243
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 234
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 355 AA; 39404 MW; 849804C5B8DC37D7 CRC64;
MHSGGTFDIP ALEAELSKFD CQMEDGSFWN DATKAQQIVG QANTIKRKLH PFLKLEKRLA
DLKEIISLAK EYEDADAAQE AASEFTEISK QLESFELLVL LDKPNDSSSC YVTINSGAGG
TEACDWAAML LRMYSRWSES KGYTVTSVDY AEGDGAGISS ATIKVEGEYA YGYLKNERGV
HRLVRISPFD SAGKRHTSFS SIDVTPEMNT DIEIDLNPAD IDIQTARSGG AGGQNVNKVE
TAVILKHKPT GIIIRCTQER SQLRNRELAL ELLKAKLYQI EEDKQKDTAE REYGEKGDIG
WGSQIRSYVF QPYQMIKDLR TGEETANISA VMDGDLDAFI EAKLKGKKKG EKIED
//
