ID A0A095Z2C6_9ACTO Unreviewed; 369 AA.
AC A0A095Z2C6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=HMPREF1628_00150 {ECO:0000313|EMBL:KGF02654.1};
OS Actinomyces sp. S4-C9.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1219581 {ECO:0000313|EMBL:KGF02654.1, ECO:0000313|Proteomes:UP000035029};
RN [1] {ECO:0000313|EMBL:KGF02654.1, ECO:0000313|Proteomes:UP000035029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4-C9 {ECO:0000313|EMBL:KGF02654.1,
RC ECO:0000313|Proteomes:UP000035029};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGF02654.1}.
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DR EMBL; JRMU01000001; KGF02654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095Z2C6; -.
DR eggNOG; COG0216; Bacteria.
DR Proteomes; UP000035029; 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 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:UP000035029}.
FT DOMAIN 236..252
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 265..307
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 243
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 369 AA; 40821 MW; 0E8DA4FE123F26E0 CRC64;
MGQDYSHELQ AVEPLLQEYR EVELQLADTQ VLGDRARSRK LAKRFSELGA VKAVADRFTQ
ALGDFEAAQE MAELDDEFAA ELPGMEQALE QAHDKLVRTL VPRDPSDADD VILEVKAGEG
GEESALFAAD LARMYTRYAE TKGWKVKELS STPTGLGGLK EISLSIASKG NVAPEDGVWA
NLKFEGGVHR VQRVPVTESQ GRVHTSAAGV IVVPEVEDDD EEIEIDQNDL RIDVYRSSGP
GGQSVNTTDS AVRITHIPSG IVVSMQNEKS QIQNREAAMR VLKARLIQKQ REEREAEEAA
VRQSQVRSMD RSERIRTYNF PENRIADHRT GYKAYNLSNV LDGDLGPVID SAIVMDEQER
MDAAGQSKE
//
