ID A0A3S0C6B3_9FLAO Unreviewed; 358 AA.
AC A0A3S0C6B3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=EHW67_12710 {ECO:0000313|EMBL:RTE53036.1};
OS Arenibacter aquaticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Arenibacter.
OX NCBI_TaxID=2489054 {ECO:0000313|EMBL:RTE53036.1, ECO:0000313|Proteomes:UP000267585};
RN [1] {ECO:0000313|EMBL:RTE53036.1, ECO:0000313|Proteomes:UP000267585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GUO666 {ECO:0000313|EMBL:RTE53036.1,
RC ECO:0000313|Proteomes:UP000267585};
RA Guo J., Sun J.;
RT "Arenibacter aquaticus sp.nov., a marine bacterium isolated from surface
RT seawater in the South China Sea.";
RL Submitted (NOV-2018) 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:RTE53036.1}.
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DR EMBL; RQPJ01000008; RTE53036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0C6B3; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000267585; 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; -; 2.
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}.
FT DOMAIN 62..177
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT REGION 287..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 358 AA; 40407 MW; D85344F8793AD68C CRC64;
MIDKLNIVKQ RFDEVSDLII QPGIIADQKR YVALNKEYKD LKQLVDKRAL YLELTNNIAE
AEEILADGSD AEMVEMAKMQ LEEAKEKLPK LEEEIKFMLI PKDPEDAKNV VVEVRAGTGG
DEASIFAGDL FRMYTKYCES KGWKTNVIDL SEGTSGGYKE IQFEVTGEDV YGTLKFEAGV
HRVQRVPQTE TQGRVHTSAA TVMVLPEAED FDVQIDPKDV RIDFFCSSGP GGQSVNTTYS
AVRLTHVPTG LVAQCQDQKS QHKNKEKAFR VLRSRLYDLE LAKKQEEDAA KRNSQVSSGD
RSAKIRTYNY PQGRVTDHRI GLTLYDLQNI INGDIQRIID ELSLVENTEK LKEASETF
//
