ID A0A3A5M7S7_9MICC Unreviewed; 359 AA.
AC A0A3A5M7S7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ECO:0000313|EMBL:RJT82247.1};
GN ORFNames=D6T63_05325 {ECO:0000313|EMBL:RJT82247.1};
OS Arthrobacter cheniae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1258888 {ECO:0000313|EMBL:RJT82247.1, ECO:0000313|Proteomes:UP000272560};
RN [1] {ECO:0000313|EMBL:RJT82247.1, ECO:0000313|Proteomes:UP000272560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hz2 {ECO:0000313|EMBL:RJT82247.1,
RC ECO:0000313|Proteomes:UP000272560};
RA Liu Q., Xin Y.-H.;
RT "Novel species of Arthrobacter.";
RL Submitted (SEP-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:RJT82247.1}.
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DR EMBL; QZVT01000002; RJT82247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A5M7S7; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000272560; 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.
DR PROSITE; PS00745; RF_PROK_I; 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 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 359 AA; 39879 MW; EADD99DEF82F0560 CRC64;
MFESIQGLLD EHSELQDQLA DPAVHADQAL ARKLGRRYAE LGRIVDAHNR WAALDDDLEA
ARGMASEDPE FAAEVPVLEE QLAVAQERLR RLLIPRDPND SRNVIIEVKG GEGGDEAALF
AGDLLRMYAR YAESRGWKTE LLSANESDLG GYKDVQMAIK GSSNDPAEGV YARLKFEGGV
HRVQRVPVTE SQGRIHTSAA GVLVLPEVDE PEEVQISQND LKIDVYRSSG PGGQSVNTTD
SAVRITHLPT GIVVAMQNEK SQLQNREAAM RVLRSRILAH EQEKIDAVNS DIRKSQIRTM
DRSERIRTYN YPENRIADHR TGYKAYNLDA VMNGELEPVV QSAIEMDEQA RLDAIGSDE
//
