ID A0A285RYN5_9RHOB Unreviewed; 351 AA.
AC A0A285RYN5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05877831_102217 {ECO:0000313|EMBL:SOB99692.1};
OS Rhodobacter maris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=446682 {ECO:0000313|EMBL:SOB99692.1, ECO:0000313|Proteomes:UP000219111};
RN [1] {ECO:0000313|Proteomes:UP000219111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA276 {ECO:0000313|Proteomes:UP000219111};
RA Varghese N., Submissions S.;
RL Submitted (AUG-2017) 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}.
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DR EMBL; OBMT01000002; SOB99692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285RYN5; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000219111; 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.
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 222..238
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 229
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 351 AA; 38884 MW; 2A4A7D688C7DBC6C CRC64;
MVPLDKLDQI TARFDFLEAK LNSALAPAEI AALSREYSDL RPVVSEIAAY RAAVSDLAEA
EGWLADPEMR DLAEEELPRL KARIPEMEQA LRIALLPKDA ADARPAILEI RPGTGGEEAA
LFAYDLWRMY ERHAERMGWR FERLDFTPTE LGGLKEGMAR IEGEGVFARL KYESGVHRVQ
RVPETEAGGR IHTSAATVAV LPEAEEVDID IPAADIRIDT MRASGAGGQH VNTTDSAVRI
THLPSGIVVT SSEKSQHQNR AIAMAVLRAR LYERERERLA TERADSRRAQ VGSGDRSERI
RTYNFPQGRM TDHRINLTLY ALPQILGGDL GEVIDALVAH DQAEKLAEMD G
//
