ID A0A1G6TKC2_9RHOB Unreviewed; 343 AA.
AC A0A1G6TKC2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-OCT-2025, entry version 25.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000256|HAMAP-Rule:MF_00093, ECO:0000256|NCBIfam:TIGR00019};
DE Short=RF-1 {ECO:0000256|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000256|HAMAP-Rule:MF_00093};
GN ORFNames=SAMN05421538_101305 {ECO:0000313|EMBL:SDD29523.1};
OS Paracoccus isoporae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Paracoccus.
OX NCBI_TaxID=591205 {ECO:0000313|EMBL:SDD29523.1, ECO:0000313|Proteomes:UP000199344};
RN [1] {ECO:0000313|EMBL:SDD29523.1, ECO:0000313|Proteomes:UP000199344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22220 {ECO:0000313|EMBL:SDD29523.1,
RC ECO:0000313|Proteomes:UP000199344};
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; FNAH01000001; SDD29523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6TKC2; -.
DR STRING; 591205.SAMN05421538_101305; -.
DR Proteomes; UP000199344; 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; -; 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; 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:UP000199344}.
FT DOMAIN 215..231
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT REGION 273..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 222
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 343 AA; 37793 MW; 35BE0173E430B95F CRC64;
MQIIQRFEFL EAKLNAGPAA DEIAEISREY ADLKPVVDQI GRWQSAREGL EEAQLMLADP
DMRELADEEV TRLKAELPLL EQALRVALLP RDAADARPAI LEIRPGTGGE EAALFAGDLL
SMYRRHSEAQ GWDFQLLEMA QTELGGVREA TVRVAGDGVF ARLKYESGVH RVQRVPETES
GGRIHTSAAT VAVLPEAQEV DIEIPAADIR IDTMRASGAG GQHVNTTDSA VRITHLPTGI
VVTSSEKSQH QNRANAMAVL RARLYDMERE RAASARAADR KSQVGSGDRS ERIRTYNFPQ
GRMTDHRINL TLYALDRVMQ GDLGEIIDAL TAHDQAERLA AQE
//
