ID A0A1I3C8Q5_9LACT Unreviewed; 359 AA.
AC A0A1I3C8Q5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-OCT-2025, entry version 24.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000256|ARBA:ARBA00050039, 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=SAMN04489868_11446 {ECO:0000313|EMBL:SFH70431.1};
OS Pisciglobus halotolerans.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
OC Carnobacteriaceae.
OX NCBI_TaxID=745365 {ECO:0000313|EMBL:SFH70431.1, ECO:0000313|Proteomes:UP000198668};
RN [1] {ECO:0000313|EMBL:SFH70431.1, ECO:0000313|Proteomes:UP000198668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27630 {ECO:0000313|EMBL:SFH70431.1,
RC ECO:0000313|Proteomes:UP000198668};
RA de Groot N.N.;
RL Submitted (OCT-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|ARBA:ARBA00004496,
CC 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}.
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DR EMBL; FOQE01000014; SFH70431.1; -; Genomic_DNA.
DR RefSeq; WP_047391849.1; NZ_FOQE01000014.1.
DR AlphaFoldDB; A0A1I3C8Q5; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000198668; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR FunFam; 3.30.160.20:FF:000004; Peptide chain release factor 1; 1.
DR FunFam; 3.30.70.1660:FF:000002; Peptide chain release factor 1; 1.
DR FunFam; 3.30.70.1660:FF:000004; Peptide chain release factor 1; 1.
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; IPR050057; Prokaryotic/Mito_RF.
DR InterPro; IPR004373; RF-1.
DR NCBIfam; TIGR00019; prfA; 1.
DR NCBIfam; NF001859; PRK00591.1; 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.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00093};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00093};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00093}; Reference proteome {ECO:0000313|Proteomes:UP000198668}.
FT DOMAIN 226..242
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 359 AA; 40561 MW; 59456A23C8DAC63E CRC64;
MFDQLESVLG RYEELNELLS DPDVISDTKR FMQLSKEEAN LRETVATYKN YKAVVEGISE
TEEMLNENLE PEMAEMAKEE LADLKGQKDE LEEKIKILML PKDENDDKNI IMEIRGAAGG
DEAQLFAGDL FSMYQRYAEA QGWKTEVMNA NITGIGGYKE ITFMITGNNV YSKLKYESGA
HRVQRVPSTE SQGRVHTSTA TVVVMPEAEE VELDLADKDI RTDIYHASGA GGQHVNKTAS
AVRLTHLPTG IVVAMQDERS QIKNREKAMK VLRARVYDQI QQEAQSEYDA ERKSAIGTGD
RSERIRTYNF PQNRVTDHRI GLTIQKLDKI LGGELDEIID ALILADQTSK LEKLKNNEY
//
