ID A0A2S0MIJ9_9BURK Unreviewed; 360 AA.
AC A0A2S0MIJ9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=C6570_16860 {ECO:0000313|EMBL:AVO35708.1};
OS Ottowia oryzae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ottowia.
OX NCBI_TaxID=2109914 {ECO:0000313|EMBL:AVO35708.1, ECO:0000313|Proteomes:UP000239709};
RN [1] {ECO:0000313|EMBL:AVO35708.1, ECO:0000313|Proteomes:UP000239709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KADR8-3 {ECO:0000313|EMBL:AVO35708.1,
RC ECO:0000313|Proteomes:UP000239709};
RA Kim S.-J., Heo J., Kwon S.-W.;
RT "Genome sequencing of Ottowia sp.";
RL Submitted (MAR-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}.
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DR EMBL; CP027666; AVO35708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0MIJ9; -.
DR KEGG; otk:C6570_16860; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000239709; Chromosome.
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 Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000239709}.
FT DOMAIN 228..244
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 264..291
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 235
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 40014 MW; 7DDE643290358868 CRC64;
MRSSLRHQLD RHAARLMELD FLLSRPDIMS DMAQFMKLSR EHTEVSAVAD RWARFQQREQ
DVAAAQDLLQ DPDMADMATE EIAAAQAELA ALEAELQRML LPKDPDDARP AFVEIRAGTG
GDESALFAGD LARMYTRYAA NQGWRVEVMS ESPAELGGYK ELVLRVDGDN VYGKLRFESG
GHRVQRVPAT ETQGRIHTSA ATVAVMPEPD EAEAIKLNPA DLRIDTFRAS GAGGQHINKT
DSAVRVVHLP TGIVAECQDG RSQHANKAQA LRVLQARLQE KERTERLAKE AATRKGLIGS
GDRSDRIRTY NFPQGRLTDH RINLTLYKLG LIMEGELQDV VDALRAAREA ELMAELEVNH
//
