ID A0A7Y7LYJ0_9MICC Unreviewed; 357 AA.
AC A0A7Y7LYJ0;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 08-OCT-2025, entry version 17.
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 ECO:0000313|EMBL:NVM94059.1};
GN ORFNames=G6034_03860 {ECO:0000313|EMBL:NVM94059.1};
OS Arthrobacter wenxiniae.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=2713570 {ECO:0000313|EMBL:NVM94059.1, ECO:0000313|Proteomes:UP000543556};
RN [1] {ECO:0000313|EMBL:NVM94059.1, ECO:0000313|Proteomes:UP000543556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AETb3-4 {ECO:0000313|EMBL:NVM94059.1,
RC ECO:0000313|Proteomes:UP000543556};
RA Gao J., Zhang X.;
RT "Genome sequence of strain AETb3-4.";
RL Submitted (FEB-2020) 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:NVM94059.1}.
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DR EMBL; JAAMFM010000003; NVM94059.1; -; Genomic_DNA.
DR RefSeq; WP_176633784.1; NZ_JAAMFM010000003.1.
DR AlphaFoldDB; A0A7Y7LYJ0; -.
DR Proteomes; UP000543556; 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:000004; Peptide chain release factor 1; 1.
DR FunFam; 3.30.70.1660:FF:000002; 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:UP000543556}.
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_00093"
SQ SEQUENCE 357 AA; 39521 MW; 01EFE9046DD9CDF7 CRC64;
MFESIHGLLD EHAELQMRLS DPAVHADQSL ARKLGRRYAE LSGVVEGYHQ VELLTDDLEA
AREMASEDPE FAAEVPVLEG QLAQAQEKLR RLLIPRDPDD ARDVILEVKA GEGGDEAALF
AADLVRMYTR YAENRGWKTE IISATESDLG GYKDISIAVK GRSNDPAEGV FARLKFEGGV
HRVQRVPATE SQGRIHTSAA GVLVLPEVDE PEEVDISQND LKIDVYRSSG PGGQSVNTTD
SAVRITHLPT GIVVAMQNEK SQLQNREAGM RVLRARILAH QQAIIDAENS AVRKSQIRTM
DRSERIRTYN YPENRIADHR TGYKAYNLDA VMNGDLEPVV QSAIEMDEQA RLDAIGD
//
