ID G5JUD6_9STRE Unreviewed; 360 AA.
AC G5JUD6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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:EHJ51806.1};
GN ORFNames=STRMA_0677 {ECO:0000313|EMBL:EHJ51806.1};
OS Streptococcus macacae NCTC 11558.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764298 {ECO:0000313|EMBL:EHJ51806.1, ECO:0000313|Proteomes:UP000003573};
RN [1] {ECO:0000313|EMBL:EHJ51806.1, ECO:0000313|Proteomes:UP000003573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 11558 {ECO:0000313|EMBL:EHJ51806.1,
RC ECO:0000313|Proteomes:UP000003573};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
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:EHJ51806.1}.
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DR EMBL; AEUW02000001; EHJ51806.1; -; Genomic_DNA.
DR RefSeq; WP_003079062.1; NZ_UHFV01000002.1.
DR AlphaFoldDB; G5JUD6; -.
DR STRING; 764298.STRMA_0677; -.
DR eggNOG; COG0216; Bacteria.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000003573; 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 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00093}.
FT DOMAIN 229..245
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 53..97
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 236
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 40587 MW; 4C80EAF675F9834D CRC64;
MNIYEQLQSV EDRYEELGEL LSDPDIVSDT KRFMELSREE AAIRETVTAY REYKKILQTI
SDAEEMLKES SDDPELEEMA KEELKTSKGA KEAYEEKLKI LLLPKDPNDD KNIILEIRGA
AGGDEAALFA GDLLAMYQKY AENQGWKFEV METSVNGVGG IKEVVAMVSG QSVYSKLKYE
SGAHRVQRVP VTESQGRVHT STATVLVMPE IEEVEYDIDP KDLRVDIYHA SGAGGQNVNK
VATAVRMIHI PTGIKVEMQE ERTQQKNRDK AMKIIRARVA DHFAQIAQDE QDAERKSTVG
TGDRSERIRT YNFPQNRVTD HRIGLTLQKL DSILSGKLDE VIDALVLYDQ TQKLEELGQG
//
