ID A0A2S7WSL0_9FLAO Unreviewed; 358 AA.
AC A0A2S7WSL0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000256|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000256|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000256|HAMAP-Rule:MF_00093};
GN ORFNames=BTO18_15960 {ECO:0000313|EMBL:PQJ80580.1};
OS Polaribacter porphyrae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1137780 {ECO:0000313|EMBL:PQJ80580.1, ECO:0000313|Proteomes:UP000238882};
RN [1] {ECO:0000313|EMBL:PQJ80580.1, ECO:0000313|Proteomes:UP000238882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108759 {ECO:0000313|EMBL:PQJ80580.1,
RC ECO:0000313|Proteomes:UP000238882};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC translation in response to the peptide chain termination codons UAG and
CC UAA. {ECO:0000256|ARBA:ARBA00002986, ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00093}.
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:PQJ80580.1}.
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DR EMBL; MSCN01000001; PQJ80580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7WSL0; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000238882; 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; 6.10.140.1950; -; 1.
DR HAMAP; MF_00093; Rel_fac_1; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004373; RF-1.
DR NCBIfam; TIGR00019; prfA; 1.
DR PANTHER; PTHR43804; LD18447P; 1.
DR PANTHER; PTHR43804:SF7; LD18447P; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00093}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00093};
KW Reference proteome {ECO:0000313|Proteomes:UP000238882}.
FT DOMAIN 63..177
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 358 AA; 40421 MW; 1AE30393D674FCF1 CRC64;
MLDKLRIVKQ RYDEVSDLII QPEIIMDQKR YAQLMKEYKD LGSVVKKGDE YNTLMNNIEE
AKEILSDGSD AEMNEMAKME IDEANARIPE LEEEIKFLLI PKDPEDSKNA VVELRAGTGG
DEASIFAGDL FRMYTKYCES KGWKVSTVDY SEGTNGGFKE IQFEVNGDDV YGTLKFEAGV
HRVQRVPQTE TQGRVHTSAA TCMVFPEAEE FDVEINPKDV RIDFFCSSGP GGQSVNTTYS
AVRLTHIPTG LVAQCQDQKS QHKNKEKAFK VLRSRLYDLE LAKKQAEDAL KRGSMVTSGD
RSAKIRTYNY PQGRVTDHRI NLTLYDLSNI VNGDIQKIID ELMLAENTEK LKELGDGI
//
